G. Abou-jaoudé and C. Sureau, Entry of Hepatitis Delta Virus Requires the Conserved Cysteine Residues of the Hepatitis B Virus Envelope Protein Antigenic Loop and Is Blocked by Inhibitors of Thiol-Disulfide Exchange, Journal of Virology, vol.81, pp.13057-13066, 2007.

S. H. Ahn, D. H. Kim, A. R. Lee, B. K. Kim, Y. K. Park et al., Substitution at rt269 in Hepatitis B Virus Polymerase Is a Compensatory Mutation Associated with Multi-Drug Resistance, PLoS ONE, vol.10, 2015.

C. Albayrak and J. R. Swartz, Cell-free co-production of an orthogonal transfer RNA activates efficient site-specific non-natural amino acid incorporation, Nucleic Acids Research, vol.41, pp.5949-5963, 2013.

A. Ali, H. Abdel-hafiz, M. Suhail, A. Al-mars, M. K. Zakaria et al., Hepatitis B virus, HBx mutants and their role in hepatocellular carcinoma, World J Gastroenterol, vol.20, pp.10238-10248, 2014.

J. G. Allen, C. Sykes, D. M. Enerson, P. V. Moulder, R. M. Elghammer et al., Homologous serum jaundice and its relation to methods of plasma storage, J Am Med Assoc, vol.144, pp.1069-1074, 1950.

M. Anastasina, I. Terenin, S. J. Butcher, and D. E. Kainov, A technique to increase protein yield in a rabbit reticulocyte lysate translation system, BioTechniques, vol.56, 2014.

L. B. Andreas, K. Jaudzems, J. Stanek, D. Lalli, A. Bertarello et al., Structure of fully protonated proteins by proton-detected magic-angle spinning NMR, Proceedings of the National Academy of Sciences, vol.113, pp.9187-9192, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01359815

P. Argos, A sequence motif in many polymerases, Nucl Acids Res, vol.16, pp.9909-9916, 1988.

R. C. Austin, R. A. Rachubinski, F. Fernandez-rachubinski, and M. A. Blajchman, Expression in a Cell-Free System of Normal and Variant Forms of Human Antithrombin 111. Ability to Bind Heparin and React With a-Thrombin, Blood, vol.76, pp.1521-1529, 1990.

M. S. Awayda, I. I. Ismailov, B. K. Berdiev, and D. J. Benos, A cloned renal epithelial Na+ channel protein displays stretch activation in planar lipid bilayers, American Journal of Physiology-Cell Physiology, vol.268, pp.1450-1459, 1995.

A. Badillo, V. Receveur-brechot, S. Sarrazin, F. Cantrelle, F. Delolme et al., Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A, Biochemistry, vol.56, pp.3029-3048, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01785410

T. Bahougne, A. Imperiale, G. Averous, G. Chabrier, A. P. Gimenez-roqueplo et al., Successful response to pegylated interferon alpha in a patient with recurrent paraganglioma, Endocrine-Related Cancer, vol.24, p.11, 2017.

Y. Bai, J. S. Milne, L. Mayne, and S. W. Englander, Primary structure effects on peptide group hydrogen exchange, Proteins, vol.17, pp.75-86, 1993.

Y. Bak, H. Shin, I. Bak, . Seon, D. Yoon et al., Hepatitis B virus X promotes hepatocellular carcinoma development via nuclear protein 1 pathway, Biochemical and Biophysical Research Communications, vol.466, pp.676-681, 2015.

R. Bartenschlager and H. Schaller, The amino-terminal domain of the hepadnaviral P-gene encodes the terminal protein (genome-linked protein) believed to prime reverse transcription, The EMBO Journal, vol.7, pp.4185-4192, 1988.

R. Bartenschlager and H. Schaller, Hepadnaviral assembly is initiated by polymerase binding to the encapsidation signal in the viral RNA genome, The EMBO Journal, vol.11, pp.3413-3420, 1992.

R. Bartenschlager, S. Urban, and U. Protzer, Towards curative therapy of chronic viral hepatitis, Zeitschrift für Gastroenterologie, vol.57, pp.61-73, 2019.

A. Bax, Multidimensional nuclear magnetic resonance methods for protein studies, Current Opinion in Structural Biology, vol.4, pp.738-744, 1994.

B. Beames and R. E. Lanford, Carboxy-terminal truncations of the HBV core protein affect capsid formation and the apparent size of encapsidated HBV RNA, Virology, vol.194, pp.597-607, 1993.

J. Beck and M. Nassal, Hepatitis B virus replication, World J Gastroenterol, vol.13, pp.48-64, 2007.

E. D. Becker, A brief history of nuclear magnetic resonance, Anal Chem, vol.65, pp.295-302, 1993.

S. A. Becker, T. Lee, J. S. Butel, and B. L. Slagle, Hepatitis B Virus X Protein Interferes with Cellular DNA Repair, J. Virol, vol.72, p.7, 1998.

G. S. Beckler, D. Thompson, and T. Van-oosbree, In Vitro Translation Using Rabbit Reticulocyte Lysate, Vitro Transcription and Translation Protocols, pp.215-232, 1995.

Y. Benhamou, H. Fleury, P. Trimoulet, I. Pellegrin, R. Urbinelli et al., Anti-hepatitis B virus efficacy of tenofovir disoproxil fumarate in HIV-infected patients, Hepatology, vol.43, pp.548-555, 2006.

J. M. Berke, P. Dehertogh, K. Vergauwen, E. Van-damme, W. Mostmans et al., Capsid Assembly Modulators Have a Dual Mechanism of Action in Primary Human Hepatocytes Infected with Hepatitis B Virus, Antimicrob. Agents Chemother, vol.61, pp.560-577, 2017.

C. Berrier, K. Park, S. Abes, A. Bibonne, J. Betton et al., , vol.43, pp.12585-12591, 2004.

I. Bertini, A. Bhaumik, G. De-paëpe, R. G. Griffin, M. Lelli et al., High-Resolution Solid-State NMR Structure of a 17.6 kDa, Protein. J. Am. Chem. Soc, vol.132, pp.1032-1040, 2010.

A. K. Bhuyan, On the mechanism of SDS-induced protein denaturation, Biopolymers, vol.93, pp.186-199, 2010.

I. T. Bijsmans, R. A. Bouwmeester, J. Geyer, K. N. Faber, and S. F. Van-de-graaf, Homo-and heterodimeric architecture of the human liver Na + -dependent taurocholate co-transporting protein, Biochem. J, vol.441, pp.1007-1016, 2012.

F. Birnbaum and M. Nassal, Hepatitis B Virus Nucleocapsid Assembly: Primary Structure Requirements in the Core Protein, Journal of Virology, vol.64, p.12, 1990.

M. Blanchet, V. Sinnathamby, A. Vaillant, and P. Labonté, Inhibition of HBsAg secretion by nucleic acid polymers in HepG2.2.15 cells, Antiviral Research, vol.164, pp.97-105, 2019.
URL : https://hal.archives-ouvertes.fr/pasteur-02133251

A. Blank, A. Eidam, M. Haag, N. Hohmann, J. Burhenne et al., The NTCP-inhibitor Myrcludex B: Effects on Bile Acid Disposition and Tenofovir Pharmacokinetics, Clin. Pharmacol. Ther, vol.103, pp.341-348, 2018.

A. Blank, C. Markert, N. Hohmann, A. Carls, G. Mikus et al., First-in-human application of the novel hepatitis B and hepatitis D virus entry inhibitor myrcludex B, Journal of Hepatology, vol.65, pp.483-489, 2016.

A. Blank, K. Meier, S. Urban, W. E. Haefeli, and J. Weiss, Drug-drug interaction potential of the hepatitis B and hepatitis D virus entry inhibitor myrcludex B assessed in vitro, Antivir Ther, vol.23, pp.267-275, 2017.

M. Blondot, V. Bruss, and M. Kann, Intracellular transport and egress of hepatitis B virus, Journal of Hepatology, vol.64, pp.49-59, 2016.

H. E. Blum, T. J. Liang, and J. R. Wands, Hepatitis B Virus X Protein Is Not Central to the Viral Life Cycle In Vitro, J. Virol, vol.66, p.5, 1992.

B. S. Blumberg, Australia antigen and the biology of hepatitis B, Science, vol.197, pp.17-25, 1977.

B. S. Blumberg, H. J. Alter, and S. Visnich, A "new" antigen in leukemia sera, JAMA, vol.191, pp.541-546, 1965.

B. S. Blumberg, A. I. Sutnick, and W. T. London, Hepatitis and leukemia: their relation to Australia antigen, Bull. N. Y. Acad. Med, vol.44, p.21, 1968.

A. Böckmann, M. Ernst, and B. H. Meier, Spinning proteins, the faster, the better?, J. Magn. Reson, vol.253, pp.71-79, 2015.

A. Böckmann, C. Gardiennet, R. Verel, A. Hunkeler, A. Loquet et al., Characterization of different water pools in solid-state NMR protein samples, J. Biomol. NMR, vol.45, pp.319-327, 2009.

O. V. Bocharova, A. S. Urban, K. D. Nadezhdin, E. V. Bocharov, and A. S. Arseniev, Cell-free expression of the APP transmembrane fragments with Alzheimer's disease mutations using algal amino acid mixture for structural NMR studies, Protein Expression and Purification, vol.123, pp.105-111, 2016.

P. Bogomolov, A. Alexandrov, N. Voronkova, M. Macievich, K. Kokina et al., Treatment of chronic hepatitis D with the entry inhibitor myrcludex B: First results of a phase Ib/IIa study, Journal of Hepatology, vol.65, pp.490-498, 2016.

C. Borel, C. Sunyach, O. Hantz, C. Trepo, K. et al., Phosphorylation of DHBV Pre-S: Identification of the Major Site of Phosphorylation and Effects of Mutations on the Virus Life Cycle, Virology, vol.242, pp.90-98, 1998.

H. Borsook, C. L. Deasy, A. J. Haagensmit, G. Keighley, and P. H. Lowy, Incorporation in vitro of labeled amino acids into proteins of rabbit reticulocytes, J Biol Chem, vol.196, pp.669-694, 1952.

B. Böttcher, S. A. Wynne, and R. A. Crowther, Determination of the fold of the core protein of hepatitis B virus by electron cryomicroscopy, Nature, vol.386, pp.88-91, 1997.

C. R. Bourne, S. P. Katen, M. R. Fulz, C. Packianathan, and A. Zlotnick, A Mutant Hepatitis B Virus Core Protein Mimics Inhibitors of Icosahedral Capsid Self-Assembly ?, Biochemistry, vol.48, pp.1736-1742, 2009.

K. M. Breiner, S. Urban, and H. Schaller, Carboxypeptidase D (gp180), a Golgi-Resident Protein, Functions in the Attachment and Entry of Avian Hepatitis B Viruses, Journal of Virology, vol.72, 1998.

C. M. Bremer, C. Bung, N. Kott, M. Hardt, and D. Glebe, Hepatitis B virus infection is dependent on cholesterol in the viral envelope, Cellular Microbiology, vol.11, pp.249-260, 2009.

Y. Chemla, E. Ozer, O. Schlesinger, V. Noireaux, A. et al., Genetically expanded cell-free protein synthesis using endogenous pyrrolysyl orthogonal translation system: Genetically expanded cell-free protein synthesis, Biotechnol. Bioeng, vol.112, pp.1663-1672, 2015.

A. Chen, N. Panjaworayan-t-thienprasert, and C. M. Brown, Prospects for inhibiting the post-transcriptional regulation of gene expression in hepatitis B virus, World J. Gastroenterol, vol.20, p.7993, 2014.

C. Chen, J. Wang, E. E. Pierson, D. Z. Keifer, M. Delaleau et al., Importin ? Can Bind Hepatitis B Virus Core Protein and Empty Core-Like Particles and Induce Structural Changes, PLoS Pathog, vol.12, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02117255

M. T. Chen, J. Billaud, M. Sallberg, L. G. Guidotti, F. V. Chisari et al., A function of the hepatitis B virus precore protein is to regulate the immune response to the core antigen, Proceedings of the National Academy of Sciences, vol.101, pp.14913-14918, 2004.

P. Chen, Y. Gan, N. Han, W. Fang, J. Li et al., Computational Evolutionary Analysis of the Overlapped Surface (S) and Polymerase (P) Region in Hepatitis B Virus Indicates the Spacer Domain in P Is Crucial for Survival, PLoS ONE, vol.8, 2013.

H. Chi, X. Wang, J. Li, H. Ren, and F. Huang, Chaperonin-enhanced Escherichia coli cell-free expression of functional CXCR4, Journal of Biotechnology, vol.231, pp.193-200, 2016.

A. C. Chiao, R. M. Murray, and Z. Z. Sun, Development of prokaryotic cell-free systems for synthetic biology, Synthetic Biology, 2016.

R. Chien and Y. Liaw, Nucleos(t)ide analogues for hepatitis B virus: Strategies for long-term success, Best Practice & Research Clinical Gastroenterology, vol.22, pp.1081-1092, 2008.

R. H. Ching, K. M. Sze, E. Y. Lau, Y. Chiu, J. M. Lee et al., C-terminal truncated hepatitis B virus X protein regulates tumorigenicity, self-renewal and drug resistance via STAT3/Nanog signaling pathway, Oncotarget, vol.8, 2017.

A. J. Clark, L. Beguinot, S. Ishii, D. P. Ma, B. A. Roe et al., Synthesis of epidermal growth factor (EGF) receptor in vitro using SP6 RNA polymerase-transcribed template mRNA, Biochimica et Biophysica Acta (BBA) -Gene Structure and Expression, vol.867, pp.244-251, 1986.

D. N. Clark, J. M. Flanagan, and J. Hu, Mapping of Functional Subdomains in the Terminal Protein Domain of Hepatitis B Virus Polymerase, J. Virol, vol.91, pp.1785-1801, 2017.

J. F. Conway, N. Cheng, A. Zlotnick, P. T. Wingfield, S. J. Stahl et al., Visualization of a 4-helix bundle in the hepatitis B virus capsid by cryo-electron microscopy, Nature, vol.386, pp.91-94, 1997.

D. Cougot, C. Neuveut, and M. A. Buendia, HBV induced carcinogenesis, Journal of Clinical Virology, vol.34, pp.80014-80023, 2005.

D. Craig, M. T. Howell, C. L. Gibbs, T. Hunt, J. et al., Plasmid cDNA-directed protein synthesis in a coupled eukaryotic in vitro transcription-translation system, Nucl Acids Res, vol.20, pp.4987-4995, 1992.

C. Cunha, J. P. Tavanez, and S. Gudima, Hepatitis delta virus: A fascinating and neglected pathogen, World Journal of Virology, vol.4, p.313, 2015.

P. R. Daga, J. Duan, and R. J. Doerksen, Computational model of hepatitis B virus DNA polymerase: Molecular dynamics and docking to understand resistant mutations, Protein Science, vol.19, pp.796-807, 2010.

V. Daniel, A. B. Maksymowych, E. S. Alnemri, and G. Litwack, Cell-free synthesis of rat glucocorticoid receptor in rabbit reticulocyte lysate. In vitro synthesis of receptor in Mr 90,000 heat shock protein-depleted lysate, J Biol Chem, vol.266, pp.1320-1325, 1991.

X. Danthinne, J. Seurinck, F. Meulewaeter, M. Van-montagu, and M. Cornelissen, , 1993.

B. B. Das, H. J. Nothnagel, G. J. Lu, W. S. Son, Y. Tian et al., Structure Determination of a Membrane Protein in Proteoliposomes, J. Am. Chem. Soc, vol.134, pp.2047-2056, 2012.

G. David, M. Fogeron, M. Schledorn, R. Montserret, U. Haselmann et al., Structural Studies of Self-Assembled Subviral Particles: Combining Cell-Free Expression with 110 kHz MAS NMR Spectroscopy, Angewandte Chemie International Edition, vol.57, pp.4787-4791, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02322342

R. J. Davis, The mitogen-activated protein kinase signal transduction pathway, J. Biol. Chem, vol.268, pp.14553-14556, 1993.

E. De-clercq, Tenofovir alafenamide (TAF) as the successor of tenofovir disoproxil fumarate (TDF), Biochemical Pharmacology, vol.119, pp.1-7, 2016.

C. De-la, L. Chen, W. Graham, B. Otting, and G. , Binding mode of the activity-modulating C-terminal segment of NS2B to NS3 in the dengue virus NS2B-NS3 protease, FEBS J, vol.281, pp.1517-1533, 2014.

C. De-pasquale and D. Kanduc, Modulation of HPV16 E7 translation by tRNAs in eukaryotic cell-free translation systems: Modulation of HPV16 E7 translation by tRNAs in eukaryotic cell-free translation systems, IUBMB Life, vol.45, pp.1005-1009, 1998.

T. Garcia, J. Li, C. Sureau, K. Ito, Y. Qin et al., Drastic Reduction in the Production of Subviral Particles Does Not Impair Hepatitis B Virus Virion Secretion, Journal of Virology, vol.83, pp.11152-11165, 2009.

E. Gasior, F. Herrera, I. Sadnik, C. S. Mclaughlin, and K. Moldave, The preparation and characterization of a cellfree system from Saccharomyces cerevisiae that translates natural messenger ribonucleic acid, J Biol Chem, vol.254, pp.3965-3969, 1979.

F. Gavilanes, J. Gomez-gutierrez, M. Aracil, J. M. Gonzalez-ros, J. A. Ferragut et al., Hepatitis B surface antigen. Role of lipids in maintaining the structural and antigenic properties of protein components, Biochemical Journal, vol.265, pp.857-864, 1990.

F. Gavilanes, J. M. Gonzalez-ros, and D. L. Peterson, Structure of hepatitis B surface antigen. Characterization of the lipid components and their association with the viral proteins, J. Biol. Chem, vol.257, pp.7770-7777, 1982.

L. Geist, M. Mayer, X. Cockcroft, B. Wolkerstorfer, D. Kessler et al., Direct NMR Probing of Hydration Shells of Protein Ligand Interfaces and Its Application to Drug Design, J. Med. Chem, vol.60, pp.8708-8715, 2017.

M. D. Gelenter, K. J. Smith, S. Liao, V. S. Mandala, A. J. Dregni et al., The peptide hormone glucagon forms amyloid fibrils with two coexisting ?-strand conformations, Nat Struct Mol Biol, vol.26, pp.592-598, 2019.

X. Geng, B. L. Harry, Q. Zhou, R. R. Skeen-gaar, X. Ge et al., Hepatitis B virus X protein targets the Bcl-2 protein CED-9 to induce intracellular Ca2+ increase and cell death in Caenorhabditis elegans, Proceedings of the National Academy of Sciences, vol.109, pp.18465-18470, 2012.

T. Genji, A. Nozawa, and Y. Tozawa, Efficient production and purification of functional bacteriorhodopsin with a wheat-germ cell-free system and a combination of Fos-choline and CHAPS detergents, Biochemical and Biophysical Research Communications, vol.400, pp.638-642, 2010.

T. Gerelsaikhan, J. E. Tavis, and V. Bruss, Hepatitis B Virus Nucleocapsid Envelopment Does Not Occur without Genomic DNA Synthesis, J. VIROL, vol.70, p.6, 1996.

E. Gerhardt and V. Bruss, Phenotypic Mixing of Rodent but Not Avian Hepadnavirus Surface Proteins into Human Hepatitis B Virus Particles, Journal of Virology, vol.69, 1995.

P. Ghersa, P. Huber, G. Semenza, and H. Wacker, Cell-free Synthesis,Membrane Integration, and Glycosylation of Pro-sucrase-isomaltase, The Journal of Biological Chemistry, vol.261, pp.7969-7974, 1986.

P. E. Gibbs, D. C. Zouzias, and I. M. Freedberg, Differential post-translational modification of human type I keratins synthesized in a rabbit reticulocyte cell-free system, Biochimica et Biophysica Acta (BBA) -Gene Structure and Expression, vol.824, pp.90055-90062, 1985.

C. Gilbert, J. M. Meik, D. Dashevsky, D. C. Card, T. A. Castoe et al., Endogenous hepadnaviruses, bornaviruses and circoviruses in snakes, Proc. R. Soc. B, vol.281, p.20141122, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01078492

R. J. Gilbert, L. Beales, D. Blond, M. N. Simon, B. Y. Lin et al., Hepatitis B small surface antigen particles are octahedral, Proc. Natl. Acad. Sci, vol.102, pp.14783-14788, 2005.

R. G. Gish, B. D. Given, C. Lai, S. A. Locarnini, J. Y. Lau et al., Chronic hepatitis B: Virology, natural history, current management and a glimpse at future opportunities, Antiviral Research, vol.121, pp.47-58, 2015.

J. Gómez-gutiérrez, I. Rodríguez-crespo, D. L. Peterson, and F. Gavilanes, Reconstitution of hepatitis B surface antigen proteins into phospholipid vesicles, Biochimica et Biophysica Acta (BBA) -Biomembranes, vol.1192, pp.45-52, 1994.

S. Goodbourn, L. Didcock, and R. E. Randall, Interferons : cell signalling, immune modulation, antiviral responses and virus countermeasures, Journal of General Virology, vol.81, pp.2341-2364, 2000.

M. A. Goren and B. G. Fox, Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex, Protein Expression and Purification, vol.62, pp.171-178, 2008.

V. J. Greiner, C. Egelé, S. Oncul, F. Ronzon, C. Manin et al., Characterization of the lipid and protein organization in HBsAg viral particles by steady-state and time-resolved fluorescence spectroscopy, Biochimie, vol.92, pp.994-1002, 2010.
URL : https://hal.archives-ouvertes.fr/hal-00508184

N. E. Gregorio, M. Z. Levine, and J. P. Oza, A User's Guide to Cell-Free Protein Synthesis, Methods Protoc, vol.2, p.24, 2019.

A. Grélard, P. Guichard, P. Bonnafous, S. Marco, O. Lambert et al., Hepatitis B subvirus particles display both a fluid bilayer membrane and a strong resistance to freeze drying: a study by solid-state NMR, light scattering, and cryoelectron microscopy/tomography, The FASEB Journal, vol.27, pp.4316-4326, 2013.

E. V. Grgacic, Virology, vol.83, pp.1635-1644, 2002.

E. V. Grgacic, A. , and D. A. , The Large Surface Protein of Duck Hepatitis B Virus Is Phosphorylated in the Pre-S Domain, J. Virol, vol.68, p.7, 1994.

E. V. Grgacic, A. , and D. A. , St, a Truncated Envelope Protein Derived from the S Protein of Duck Hepatitis B Virus, Acts as a Chaperone for the Folding of the Large Envelope Protein, Journal of Virology, vol.79, pp.5346-5352, 2005.

E. V. Grgacic, D. A. Anderson, B. Lin, M. J. Snooks, and E. V. Gazina, Normal phosphorylation of duck hepatitis B virus L protein is dispensable for infectivity, Journal of General Virology, vol.79, pp.2743-2751, 1998.

P. Gripon, S. Rumin, S. Urban, J. L. Seyec, D. Glaise et al., Infection of a human hepatoma cell line by hepatitis B virus, Proceedings of the National Academy of Sciences, vol.99, pp.15655-15660, 2002.

F. Guo, Q. Zhao, M. Sheraz, J. Cheng, Y. Qi et al., HBV core protein allosteric modulators differentially alter cccDNA biosynthesis from de novo infection and intracellular amplification pathways, PLoS Pathog, vol.13, 2017.

H. Guo, W. S. Mason, C. E. Aldrich, J. R. Saputelli, D. S. Miller et al., Identification and Characterization of Avihepadnaviruses Isolated from Exotic Anseriformes Maintained in Captivity, Journal of Virology, vol.79, pp.2729-2742, 2005.

J. Guo and J. C. Pugh, Topology of the Large Envelope Protein of Duck Hepatitis B Virus Suggests a Mechanism for Membrane Translocation during Particle Morphogenesis, J. Virol, vol.71, 1997.

M. Harbers, Wheat germ systems for cell-free protein expression, FEBS Letters, vol.588, pp.2762-2773, 2014.

E. Hardy, E. Mart??ez, D. Diago, R. D?áz, D. González et al., Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris, Journal of Biotechnology, vol.77, pp.157-167, 2000.

Z. D. Harms, D. G. Haywood, A. R. Kneller, L. Selzer, A. Zlotnick et al., Single-Particle Electrophoresis in Nanochannels, Anal. Chem, vol.87, pp.699-705, 2015.

R. K. Harris, E. D. Becker, R. Goodfellow, and P. Granger, NMR nomenclature. Nuclear spin properties and conventions for chemical shifts, Pure and Applied Chemistry, p.24, 2001.

J. Hayer, F. Jadeau, G. Deleage, A. Kay, F. Zoulim et al., HBVdb: a knowledge database for Hepatitis B Virus, Nucleic Acids Research, vol.41, 2013.
URL : https://hal.archives-ouvertes.fr/hal-00965883

L. He, B. Bardiaux, M. Ahmed, J. Spehr, R. König et al., Structure determination of helical filaments by solid-state NMR spectroscopy, Proc Natl Acad Sci, vol.113, pp.272-281, 2016.
URL : https://hal.archives-ouvertes.fr/pasteur-01501716

P. He, B. Zhang, D. Liu, X. Bian, D. Li et al., Hepatitis B Virus X Protein Modulates Apoptosis in NRK-52E Cells and Activates Fas/FasL Through the MLK3-MKK7-JNK3 Signaling Pathway, vol.39, pp.1433-1443, 2016.

K. H. Heermann, U. Goldmann, W. Schwartz, T. Seyffarth, H. Baumgarten et al., Large surface proteins of hepatitis B virus containing the pre-s sequence, J Virol, vol.52, pp.396-402, 1984.

K. O. Hensel, J. C. Rendon, M. Navas, M. G. Rots, and J. Postberg, Virus-host interplay in hepatitis B virus infection and epigenetic treatment strategies, FEBS J, vol.284, pp.3550-3572, 2017.

C. F. Heredia and H. O. Halvorson, Transfer of, Amino Acids from Aminoacyl Soluble Ribonucleic Acid to Protein by Cell-Free Extracts from Yeast * . Biochemistry, vol.5, pp.946-952, 1966.

R. O. Heuckeroth, D. A. Towler, S. P. Adams, L. Glaser, G. et al., 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase, J. Biol. Chem, vol.263, pp.2127-2133, 1988.

M. R. Hilleman, W. J. Mcaleer, E. B. Buynak, and A. A. Mclean, The preparation and safety of hepatitis B vaccine, Journal of Infection, vol.7, pp.3-8, 1983.

M. Hino, M. Kataoka, K. Kajimoto, T. Yamamoto, J. Kido et al., Efficiency of cell-free protein synthesis based on a crude cell extract from Escherichia coli, wheat germ, and rabbit reticulocytes, Journal of Biotechnology, vol.133, pp.183-189, 2008.

S. Hirose, Y. Kawamura, K. Yokota, T. Kuroita, T. Natsume et al., Biochemistry, vol.150, pp.73-81, 2011.

A. J. Hodgson, J. M. Hyser, V. V. Keasler, Y. Cang, and B. L. Slagle, Hepatitis B virus regulatory HBx protein binding to DDB1 is required but is not sufficient for maximal HBV replication, Virology, vol.426, pp.73-82, 2012.

N. E. Holden, T. B. Coplen, J. K. Böhlke, L. V. Tarbox, J. Benefield et al., IUPAC Periodic Table of the Elements and Isotopes (IPTEI) for the Education Community, vol.90, pp.1833-2092, 2019.

S. H. Hong, Y. Kwon, R. W. Martin, B. J. Des-soye, A. M. De-paz et al., Improving Cell-Free Protein Synthesis through Genome Engineering of Escherichia coli Lacking Release Factor 1, ChemBioChem, vol.16, pp.844-853, 2015.

F. A. Hopf, R. F. Shea, and M. O. Scully, Theory of Optical Free-Induction Decay and Two-Photon Superradiance, Phys. Rev. A, vol.7, pp.2105-2110, 1973.

J. Hu and K. Liu, Complete and Incomplete Hepatitis B Virus Particles: Formation, Function, and Application, vol.9, p.56, 2017.

H. Huang, C. Chen, W. Chang, M. Tao, and C. Huang, Entry of Hepatitis B Virus into Immortalized Human Primary Hepatocytes by Clathrin-Dependent Endocytosis, Journal of Virology, vol.86, pp.9443-9453, 2012.

M. Huang and J. Summers, Infection Initiated by the RNA Pregenome of a DNA Virus, Journal of Virology, vol.65, 1991.

Z. Huang, Y. , and T. S. , Hepatitis B Virus RNA Element That Facilitates Accumulation of Surface Gene Transcripts in the Cytoplasm, Journal of Virology, vol.68, 1994.

A. P. Huovila, A. M. Eder, and S. D. Fuller, Hepatitis B surface antigen assembles in a post-ER, pre-Golgi compartment, The Journal of Cell Biology, vol.118, pp.1305-1320, 1992.

R. Hurwitz, Milestones in magnetic resonance: 'A new method of measuring nuclear magnetic moment, J. Magn. Reson. Imaging, vol.2, pp.131-133, 1992.

M. Hussain and A. S. Lok, Mutations in the hepatitis B virus polymerase gene associated with antiviral treatment for hepatitis B, Journal of Viral Hepatitis, vol.6, pp.183-194, 1999.

S. Hwang, P. Fricke, M. Zinke, K. Giller, J. S. Wall et al., Comparison of the 3D structures of mouse and human ?-synuclein fibrils by solid-state NMR and STEM, Journal of Structural Biology, vol.206, pp.43-48, 2019.

, International Committee on Taxonomy of Viruses (ICTV), ICTV Ninth Report, 2009.

T. Inoue and Y. Tanaka, Hepatitis B virus and its sexually transmitted infection -an update, vol.3, pp.419-436, 2016.

L. Isaksson, J. Enberg, R. Neutze, B. Göran-karlsson, and A. Pedersen, Expression screening of membrane proteins with cell-free protein synthesis, Protein Expression and Purification, vol.82, pp.218-225, 2012.

Y. Ishii, A. Wickramasinghe, I. Matsuda, Y. Endo, Y. Ishii et al., Progress in proton-detected solidstate NMR (SSNMR): Super-fast 2D SSNMR collection for nano-mole-scale proteins, Journal of Magnetic Resonance, vol.286, pp.99-109, 2018.

K. Ito, K. Kim, A. S. Lok, .. Tong, and S. , Characterization of Genotype-Specific Carboxyl-Terminal Cleavage Sites of Hepatitis B Virus e Antigen Precursor and Identification of Furin as the Candidate Enzyme, Journal of Virology, vol.83, pp.3507-3517, 2009.

K. Ito, Y. Qin, M. Guarnieri, T. Garcia, K. Kwei et al., Impairment of Hepatitis B Virus Virion Secretion by Single-Amino-Acid Substitutions in the Small Envelope Protein and Rescue by a Novel Glycosylation Site, Journal of Virology, vol.84, pp.12850-12861, 2010.

M. Iwamoto, W. Saso, R. Sugiyama, K. Ishii, M. Ohki et al., Epidermal growth factor receptor is a host-entry cofactor triggering hepatitis B virus internalization, Proc Natl Acad Sci, vol.116, pp.8487-8492, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02370743

R. C. Jackson and G. Blobel, Post-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity, Proceedings of the National Academy of Sciences, vol.74, pp.5598-5602, 1977.

T. Jaroentomeechai, J. C. Stark, A. Natarajan, C. J. Glasscock, L. E. Yates et al., Single-pot glycoprotein biosynthesis using a cell-free transcription-translation system enriched with glycosylation machinery, Nature Communications, vol.9, p.2686, 2018.

C. P. Jaroniec, C. E. Macphee, V. S. Bajaj, M. T. Mcmahon, C. M. Dobson et al., High-resolution molecular structure of a peptide in an amyloid fibril determined by magic angle spinning NMR spectroscopy, Proceedings of the National Academy of Sciences, vol.101, pp.711-716, 2004.

S. Jekhmane, J. Medeiros-silva, J. Li, F. Kummerer, C. Muller-hermes et al., Shifts in the selectivity filter dynamics cause modal gating in K(+) channels, Nat Commun, vol.10, p.123, 2019.

D. Jeong, M. Klocke, S. Agarwal, J. Kim, S. Choi et al., Cell-Free Synthetic Biology Platform for Engineering Synthetic Biological Circuits and Systems, Methods Protoc, vol.2, p.39, 2019.

M. C. Jewett and J. R. Swartz, Mimicking the Escherichia coli cytoplasmic environment activates long-lived and efficient cell-free protein synthesis, Biotechnol. Bioeng, vol.86, pp.19-26, 2004.

B. Jiang, K. Himmelsbach, H. Ren, K. Boller, and E. Hildt, Subviral Hepatitis B Virus Filaments, like Infectious Viral Particles, Are Released via Multivesicular Bodies, Journal of Virology, vol.90, pp.3330-3341, 2016.

L. Jiang, J. Zhao, J. Lian, and Z. Xu, Cell-free protein synthesis enabled rapid prototyping for metabolic engineering and synthetic biology, Synthetic and Systems Biotechnology, vol.3, pp.90-96, 2018.

K. Kuroki, R. Russnak, and D. Ganem, Novel N-terminal amino acid sequence required for retention of a hepatitis B virus glycoprotein in the endoplasmic reticulum, Mol. Cell. Biol, vol.9, pp.4459-4466, 1989.

M. Kurosaki, N. Enomoto, Y. Asahina, I. Sakuma, T. Ikeda et al., Mutations in the core promoter region of hepatitis B virus in patients with chronic hepatitis B, Journal of Medical Virology, vol.49, pp.115-123, 1996.

A. Kurotani, T. Takagi, M. Toyama, M. Shirouzu, S. Yokoyama et al., Comprehensive bioinformatics analysis of cell-free protein synthesis: identification of multiple protein properties that correlate with successful expression, The FASEB Journal, vol.24, pp.1095-1104, 2010.

H. Kusunoki, T. Tanaka, T. Kohno, H. Kimura, K. Hosoda et al., Expression, purification and characterization of hepatitis B virus X protein BH3-like motif-linker-Bcl-xL fusion protein for structural studies, Biochemistry and Biophysics Reports, vol.9, pp.159-165, 2017.

H. Kusunoki, T. Tanaka, T. Kohno, K. Wakamatsu, and I. Hamaguchi, Structural characterization of the BH3-like motif of hepatitis B virus X protein, Biochemical and Biophysical Research Communications, vol.450, pp.741-745, 2014.

K. Kwei, X. Tang, A. S. Lok, C. Sureau, T. Garcia et al., Impaired Virion Secretion by Hepatitis B Virus Immune Escape Mutants and Its Rescue by Wild-Type Envelope Proteins or a Second-Site Mutation, Journal of Virology, vol.87, pp.2352-2357, 2013.

Y. Kwon and M. C. Jewett, High-throughput preparation methods of crude extract for robust cell-free protein synthesis, Sci Rep, vol.5, p.8663, 2015.

D. Lacabanne, M. Fogeron, T. Wiegand, R. Cadalbert, B. H. Meier et al., Protein sample preparation for solid-state NMR investigations, Progress in Nuclear Magnetic Resonance Spectroscopy, vol.110, pp.20-33, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02322535

D. Lacabanne, B. H. Meier, and A. Böckmann, Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy, Journal of Biomolecular NMR, vol.71, pp.141-150, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02322201

A. Laganowsky, E. Reading, T. M. Allison, M. B. Ulmschneider, M. T. Degiacomi et al., Membrane proteins bind lipids selectively to modulate their structure and function, Nature, vol.510, pp.172-175, 2014.

A. Laguerre, F. Löhr, F. Bernhard, and V. Dötsch, Labeling of Membrane Proteins by Cell-Free Expression, Methods in Enzymology, pp.367-388, 2015.

L. Lai, C. Hui, N. Leung, and G. K. Lau, Pegylated interferon alpha-2a (40 kDa) in the treatment of chronic hepatitis B, International Journal of Nanomedicine, vol.1, pp.255-262, 2006.

C. Lambert and R. Prange, Dual Topology of the Hepatitis B Virus Large Envelope Protein: Determinants Influencing Post-Translational Pre-S Translocation, J. Biol. Chem, vol.276, pp.22265-22272, 2001.

C. Lambert and R. Prange, Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation, Proceedings of the National Academy of Sciences, vol.100, pp.5199-5204, 2003.

C. Lambert, T. Doring, and R. Prange, Hepatitis B Virus Maturation Is Sensitive to Functional Inhibition of ESCRT-III, Vps4, and 2-Adaptin, Journal of Virology, vol.81, pp.9050-9060, 2007.

M. R. Lamborg and P. C. Zamecnik, Amino acid incorporation into protein by extracts of E. coli, Biochimica et Biophysica Acta, vol.42, pp.90782-90786, 1960.

P. Lampertico, K. Agarwal, T. Berg, M. Buti, H. L. Janssen et al., Clinical Practice Guidelines on the management of hepatitis B virus infection, Journal of Hepatology, vol.67, pp.370-398, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01795719

T. Lang, C. Lo, N. Skinner, S. Locarnini, K. Visvanathan et al., The Hepatitis B e antigen (HBeAg) targets and suppresses activation of the Toll-like receptor signaling pathway, Journal of Hepatology, vol.55, pp.762-769, 2011.

B. A. Larder, D. J. Purifoy, K. L. Powell, D. , and G. , Site-specific mutagenesis of AIDS virus reverse transcriptase, Nature, vol.327, pp.716-717, 1987.

I. Larrieu, J. Tolchard, C. Sanchez, E. Y. Kone, A. Barras et al., Cell-Free Expression for the Study of Hydrophobic Proteins: The Example of Yeast, Methods Mol Biol, vol.1635, pp.57-90, 2017.

C. Lauber, S. Seitz, S. Mattei, A. Suh, J. Beck et al., Deciphering the Origin and Evolution of Hepatitis B Viruses by Means of a Family of Non-enveloped Fish Viruses, Cell Host & Microbe, vol.22, pp.387-399, 2017.

D. Lavanchy, Hepatitis B virus epidemiology, disease burden, treatment, and current and emerging prevention and control measures, J Viral Hepat, vol.11, pp.97-107, 2004.

M. Le-maire, P. Champeil, and J. V. Møller, Interaction of membrane proteins and lipids with solubilizing detergents, Biochimica et Biophysica Acta (BBA) -Biomembranes, vol.1508, pp.86-111, 2000.

L. Sage, V. Mouland, and A. , Viral Subversion of the Nuclear Pore Complex, Viruses, vol.5, pp.2019-2042, 2013.

L. Lecoq, M. Schledorn, S. Wang, S. Smith-penzel, A. A. Malär et al., 100 kHz MAS Proton-Detected NMR Spectroscopy of Hepatitis B Virus Capsids. Front, Mol. Biosci, vol.6, p.58, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02322643

L. Lecoq, S. Wang, T. Wiegand, S. Bressanelli, M. Nassal et al., Localizing Conformational Hinges by NMR: Where Do Hepatitis B Virus Core Proteins Adapt for Capsid Assembly?, ChemPhysChem, vol.19, pp.1336-1340, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02180793

H. W. Lee, J. Y. Park, and S. H. Ahn, An evaluation of entecavir for the treatment of chronic hepatitis B infection in adults, Expert Review of Gastroenterology & Hepatology, vol.10, pp.177-186, 2016.

H. Lee, H. Jeong, S. Y. Lee, S. S. Kim, and K. L. Jang, Hepatitis B Virus X Protein Stimulates Virus Replication Via DNA Methylation of the C-1619 in Covalently Closed Circular DNA, Molecules and Cell, p.12, 2019.

C. M. Leistner, S. Gruen-bernhard, and D. Glebe, Role of glycosaminoglycans for binding and infection of hepatitis B virus, Cell Microbiol, vol.0, p.070810224957001, 2007.

J. R. Lewandowski, J. Dumez, Ü. Akbey, S. Lange, L. Emsley et al., Enhanced Resolution and Coherence Lifetimes in the Solid-State NMR Spectroscopy of Perdeuterated Proteins under Ultrafast Magic-Angle Spinning, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00700385

, J. Phys. Chem. Lett, vol.2, pp.2205-2211

E. B. Lewellyn and D. D. Loeb, The Arginine Clusters of the Carboxy-Terminal Domain of the Core Protein of Hepatitis B Virus Make Pleiotropic Contributions to Genome Replication, Journal of Virology, vol.85, pp.1298-1309, 2011.

J. Li and S. Tong, From DCPD to NTCP: The long journey towards identifying a functional hepatitis B virus receptor. Clinical and Molecular Hepatology 21, p.193, 2015.

W. Li, The Hepatitis B Virus Receptor, Annu. Rev. Cell Dev. Biol, vol.31, pp.125-147, 2015.

W. Li and S. Urban, Entry of hepatitis B and hepatitis D virus into hepatocytes: Basic insights and clinical implications, Journal of Hepatology, vol.64, 2016.

Y. Li, Y. Ren, H. Fu, L. Zou, Y. Yang et al., Hepatitis B Virus Middle Protein Enhances IL-6, 2016.

, Production via p38 MAPK/NF-?B Pathways in an ER Stress-Dependent Manner, PLoS ONE, vol.11

J. Lien, D. J. Petcu, C. E. Aldrich, and W. S. Mason, Initiation and Termination of Duck Hepatitis B Virus DNA Synthesis during Virus Maturation, Journal of Virology, vol.61, p.9, 1987.

C. S. Lim and C. M. Brown, Hepatitis B virus nuclear export elements: RNA stem-loop ? and ?, key parts of the HBV post-transcriptional regulatory element, RNA Biology, vol.13, pp.743-747, 2016.

H. J. Lim and D. Kim, Cell-Free Metabolic Engineering: Recent Developments and Future Prospects, Methods Protoc, vol.2, p.33, 2019.

A. Lindblom and L. Fransson, Endothelial heparan sulphate: Compositional analysis and comparison of chains from different proteoglycan populations, Glycoconjugate J, vol.7, pp.545-562, 1990.

J. R. Lingappa, R. L. Hill, M. L. Wong, and R. S. Hegde, A Multistep, ATP-dependent Pathway for Assembly of Human Immunodeficiency Virus Capsids in a Cell-free System, J Cell Biol, vol.136, pp.567-581, 1997.

U. F. Lingappa, X. Wu, A. Macieik, S. F. Yu, A. Atuegbu et al., Host-rabies virus protein-protein interactions as druggable antiviral targets, Proceedings of the National Academy of Sciences, vol.110, pp.861-868, 2013.

V. R. Lingappa, J. R. Lingappa, R. Prasad, K. E. Ebner, and G. Blobel, Coupled cell-free synthesis, segregation, and core glycosylation of a secretory protein, Proceedings of the National Academy of Sciences, vol.75, pp.2338-2342, 1978.

J. W. Littlefield and E. B. Keller, Incorporation of C14-amino acids into ribonucleoprotein particles from the Ehrlich mouse ascites tumor, J Biol Chem, vol.224, pp.13-30, 1957.

C. Liu, G. Xu, Z. Gao, Z. Zhou, G. Guo et al., , 2018.

K. Liu, L. Luckenbaugh, X. Ning, J. Xi, and J. Hu, Multiple roles of core protein linker in hepatitis B virus replication, PLoS Pathog, vol.14, 2018.

N. Liu, J. Zhang, X. Yang, T. Jiao, X. Zhao et al., HDM2 Promotes NEDDylation of Hepatitis B Virus HBx To Enhance Its Stability and Function, J. Virol, vol.91, pp.340-357, 2017.

Q. Liu, M. Somiya, N. Shimada, W. Sakamoto, N. Yoshimoto et al., Mutational analysis of hepatitis B virus pre-S1 (9-24) fusogenic peptide, Biochemical and Biophysical Research Communications, vol.474, pp.406-412, 2016.

R. A. Lizzano, B. Yang, A. J. Clippinger, and M. J. Bouchard, The C-terminal region of the hepatitis B virus X protein is essential for its stability and function, Virus Research, vol.155, pp.231-239, 2011.

A. S. Lok, F. Zoulim, G. Dusheiko, and M. G. Ghany, Hepatitis B cure: From discovery to regulatory approval, Hepatology, vol.66, pp.1296-1313, 2017.

A. R. Long, C. C. O'brien, and N. N. Alder, The Cell-Free Integration of a Polytopic Mitochondrial Membrane Protein into Liposomes Occurs Cotranslationally and in a Lipid-Dependent Manner, PLoS ONE, vol.7, p.46332, 2012.

Q. Long, R. Yan, J. Hu, D. Cai, B. Mitra et al., The role of host DNA ligases in hepadnavirus covalently closed circular DNA formation, PLoS Pathog, vol.13, 2017.

J. L. Lopes, D. C. Oliveira, C. L. Utescher, W. Quintilio, E. C. Tenório et al., Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions, Vaccine, vol.37, pp.6415-6425, 2019.

A. Loquet, B. Bardiaux, C. Gardiennet, C. Blanchet, M. Baldus et al., 3D Structure Determination of the Crh Protein from Highly Ambiguous Solid-State NMR Restraints, J. Am. Chem. Soc, vol.130, pp.3579-3589, 2008.
URL : https://hal.archives-ouvertes.fr/hal-00315184

M. Loriot, P. Marcellin, F. Walker, N. Boyer, C. Degott et al., Persistence of hepatitis B virus DNA in serum and liver from patients with chronic hepatitis B after loss of HBsAG, Journal of Hepatology, vol.27, pp.80168-80175, 1997.

G. J. Lu, Y. Tian, N. Vora, F. M. Marassi, and S. J. Opella, The Structure of the Mercury Transporter MerF in Phospholipid Bilayers: A Large Conformational Rearrangement Results from N-Terminal Truncation, J. Am. Chem. Soc, vol.135, pp.9299-9302, 2013.

S. X. Lu and E. M. Hrabak, An Arabidopsis Calcium-Dependent Protein Kinase Is Associated with the Endoplasmic Reticulum, Plant Physiol, vol.128, pp.1008-1021, 2002.

J. Lucifora, S. Arzberger, D. Durantel, L. Belloni, M. Strubin et al., Hepatitis B virus X protein is essential to initiate and maintain virus replication after infection, Journal of Hepatology, vol.55, pp.996-1003, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00850162

N. Luckgei, A. K. Schütz, B. Habenstein, L. Bousset, Y. Sourigues et al., Solid-state NMR sequential assignments of the amyloid core of Sup35pNM, Biomol NMR Assign, vol.8, pp.365-370, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01181118

L. Ludgate, K. Liu, L. Luckenbaugh, N. Streck, S. Eng et al., Cell-Free Hepatitis B Virus Capsid Assembly Dependent on the Core Protein C-Terminal Domain and Regulated by Phosphorylation, Journal of Virology, vol.90, pp.5830-5844, 2016.

L. Ludgate, K. Liu, L. Luckenbaugh, N. Streck, S. Eng et al., Cell-Free Hepatitis B Virus Capsid Assembly Dependent on the Core Protein C-Terminal Domain and Regulated by Phosphorylation, Journal of Virology, vol.90, pp.5830-5844, 2016.

L. K. Lyford and R. L. Rosenberg, Cell-free Expression and Functional Reconstitution of Homo-oligomeric ?7, 1999.

, Nicotinic Acetylcholine Receptors into Planar Lipid Bilayers, The Journal of Biological Chemistry, vol.274, pp.25675-25681

E. N. Lyukmanova, Z. O. Shenkarev, N. F. Khabibullina, G. S. Kopeina, M. A. Shulepko et al., , 2012.

, Lipid-protein nanodiscs for cell-free production of integral membrane proteins in a soluble and folded state: Comparison with detergent micelles, bicelles and liposomes, Biochimica et Biophysica Acta (BBA) -Biomembranes, vol.1818, pp.349-358

H. Mabit and H. Schaller, Intracellular Hepadnavirus Nucleocapsids Are Selected for Secretion by Envelope Protein-Independent Membrane Binding, Journal of Virology, vol.74, pp.11472-11478, 2000.

A. Macovei, C. Petrareanu, C. Lazar, P. Florian, and N. Branza-nichita, Regulation of Hepatitis B Virus Infection by Rab5, Rab7, and the Endolysosomal Compartment, Journal of Virology, vol.87, pp.6415-6427, 2013.

A. Macovei, C. Radulescu, C. Lazar, S. Petrescu, D. Durantel et al., Hepatitis B Virus Requires Intact Caveolin-1 Function for Productive Infection in HepaRG Cells, Journal of Virology, vol.84, pp.243-253, 2010.

D. R. Macrae, V. Bruss, and D. Ganem, Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly, Virology, vol.181, pp.359-363, 1991.

K. Madin, T. Sawasaki, T. Ogasawara, and Y. Endo, A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos: Plants apparently contain a suicide system directed at ribosomes, Proceedings of the National Academy of Sciences, vol.97, pp.559-564, 2000.

C. Maenz, S. Chang, A. Iwanski, and M. Bruns, Entry of Duck Hepatitis B Virus into Primary Duck Liver and Kidney Cells after Discovery of a Fusogenic Region within the Large Surface Protein, Journal of Virology, vol.81, pp.5014-5023, 2007.

C. Maenz, C. Loscher, A. Iwanski, and M. Bruns, Inhibition of duck hepatitis B virus infection of liver cells by combined treatment with viral e antigen and carbohydrates, Journal of General Virology, p.11, 2019.

Y. Mak, D. J. Skylas, R. Willows, A. Connolly, S. J. Cordwell et al., A proteomic approach to the identification and characterisation of protein composition in wheat germ, Functional & Integrative Genomics, vol.6, pp.322-337, 2006.

V. S. Mandala and M. Hong, High-sensitivity protein solid-state NMR spectroscopy, Curr. Opin. Struct. Biol, vol.58, pp.183-190, 2019.

E. Mandart, A. Kay, and F. Galibert, Nucleotide Sequence of a Cloned Duck Hepatitis B Virus Genome: Comparison with Woodchuck and Human Hepatitis B Virus Sequences, Journal of Virology, vol.49, pp.782-792, 1984.

C. M. Mangold and R. E. Streeck, Mutational Analysis of the Cysteine Residues in the Hepatitis B Virus Small Envelope Protein, Journal of Virology, vol.67, p.10, 1993.

C. M. Mangold, F. Unckell, M. Werr, and R. E. Streeck, Analysis of intermolecular disulfide bonds and free sulfhydryl groups in hepatitis B surface antigen particles, Archives of Virology, vol.142, pp.2257-2267, 1997.

C. M. Mangold, F. Unckell, M. Werr, and R. E. Streeck, Secretion and antigenicity of hepatitis B virus small envelope proteins lacking cysteines in the major antigenic region, Virology, vol.211, pp.535-543, 1995.

G. Manning, The Protein Kinase Complement of the Human Genome, Science, vol.298, pp.1912-1934, 2002.

T. Manolikas, T. Herrmann, and B. H. Meier, Protein Structure Determination from 13 C Spin-Diffusion Solid-State NMR Spectroscopy, J. Am. Chem. Soc, vol.130, pp.3959-3966, 2008.

K. Marcu and B. Dudock, Characterization of a highly efficient protein synthesizing system derived from commercial wheat germ, Nucl Acids Res, vol.1, pp.1385-1398, 1974.

P. L. Marion, S. S. Knight, M. A. Feitelson, &. Robinson, and W. S. , Major Polypeptide of Duck Hepatitis B Surface Antigen Particles, Journal of Virology, vol.48, 1983.

P. L. Marion, L. S. Oshiro, D. C. Regnery, G. H. Scullard, R. et al., A virus in Beechey ground squirrels that is related to hepatitis B virus of humans, Proceedings of the National Academy of Sciences, vol.77, pp.2941-2945, 1980.

S. Martin-vilchez, E. Lara-pezzi, M. Trapero-marugán, R. Moreno-otero, and P. Sanz-cameno, The molecular and pathophysiological implications of hepatitis B X antigen in chronic hepatitis B virus infection: HBx-related liver pathophysiology mechanisms, Rev. Med. Virol, 2011.

I. Maslennikov, C. Klammt, E. Hwang, G. Kefala, M. Okamura et al., Membrane domain structures of three classes of histidine kinase receptors by cell-free expression and rapid NMR analysis, Proceedings of the National Academy of Sciences, vol.107, pp.10902-10907, 2010.

W. S. Mason, Animal Models and the Molecular Biology of Hepadnavirus Infection, Cold Spring Harbor Perspectives in Medicine, vol.5, pp.21352-021352, 2015.

W. S. Mason, J. Cullen, J. Saputelli, T. Wu, C. Liu et al., Characterization of the antiviral effects of 2? carbodeoxyguanosine in ducks chronically infected with duck hepatitis B virus, Hepatology, vol.19, pp.398-411, 1994.

W. S. Mason, G. Seal, and J. Summers, Virus of Pekin Ducks with Structural and Biological Relatedness to Human Hepatitis B Virus, Journal of Virology, vol.36, pp.829-836, 1980.

S. Matsunaga, S. Kawakami, I. Matsuo, A. Okayama, H. Tsukagoshi et al., , 2014.

A. Maughan and O. Ogbuagu, Pegylated interferon alpha 2a for the treatment of hepatitis C virus infection, Expert Opinion on Drug Metabolism & Toxicology, vol.14, pp.219-227, 2018.

P. Maupas, A. Goudeau, P. Coursaget, J. Drucker, P. Bagros et al., Vaccine against hepatitis B -18 months prevention in a high risk setting, Med Microbiol Immunol, vol.166, pp.109-118, 1978.

A. Mcdermott, T. Polenova, A. Böckmann, K. W. Zilm, R. W. Martin et al., Partial NMR assignments for uniformly (13C, 15N)-enriched BPTI in the solid state, J. Biomol. NMR, vol.16, pp.209-2019, 2000.
URL : https://hal.archives-ouvertes.fr/hal-00314371

L. P. Mcintosh and F. W. Dahlquist, Biosynthetic Incorporation of 15 N and 13 C for Assignment and Interpretation of Nuclear Magnetic Resonance Spectra of Proteins, Quart. Rev. Biophys, vol.23, pp.1-38, 1990.

A. Mclachlan, D. R. Milich, A. K. Raney, M. G. Riggs, J. L. Hughes et al., Expression of Hepatitis B Virus Surface and Core Antigens: Influences of Pre-S and Precore Sequencest, Journal of Virology, vol.61, pp.683-692, 1987.

A. L. Mcnaughton, V. D'arienzo, M. A. Ansari, S. F. Lumley, M. Littlejohn et al., Insights From Deep Sequencing of the HBV Genome-Unique, Tiny, and Misunderstood, Gastroenterology, vol.156, pp.384-399, 2019.

D. A. Mead, E. S. Skorupa, and B. Kemper, Single stranded DNA SP6 promoter plasmids for engineering mutant RNAs and proteins: synthesis of a 'stretched' preproparathyroid hormone, Nucl Acids Res, vol.13, pp.1103-1118, 1985.

P. Meier, C. A. Scougall, H. Will, C. J. Burrell, and A. R. Jilbert, A duck hepatitis B virus strain with a knockout mutation in the putative X ORF shows similar infectivity and in vivo growth characteristics to wild-type virus, Virology, vol.317, 2003.

M. Melegari, P. P. Scaglioni, and J. R. Wands, Hepatitis B virus mutants associated with 3TC and famciclovir administration are replication defective, Hepatology, vol.27, pp.628-633, 1998.

F. Messageot, S. Salhi, P. Eon, and J. Rossignol, Proteolytic Processing of the Hepatitis B Virus e Antigen Precursor: CLEAVAGE AT TWO FURIN CONSENSUS SEQUENCES, J. Biol. Chem, vol.278, pp.891-895, 2003.

M. Mhamdi, A. Funk, H. Hohenberg, W. , and H. , Assembly and budding of a hepatitis B virus is mediated by a novel type of intracellular vesicles, Hepatology, vol.46, p.12, 2007.

N. Michel-reydellet, K. Calhoun, and J. Swartz, Amino acid stabilization for cell-free protein synthesis by modification of the Escherichia coli genome, Metabolic Engineering, vol.6, pp.197-203, 2004.

E. Michel and K. Wüthrich, Cell-free expression of disulfide-containing eukaryotic proteins for structural biology: Cell-free expression of disulfide-containing proteins, FEBS Journal, vol.279, pp.3176-3184, 2012.

L. A. Miles, G. A. Crespi, S. Han, A. F. Hill, and M. W. Parker, An Escherichia coli Cell-Free System for Recombinant Protein Synthesis on a Milligram Scale, Protein Folding, Misfolding, and Disease, pp.17-28, 2011.

R. H. Miller, R. , and W. S. , Common evolutionary origin of hepatitis B virus and retroviruses, Proceedings of the National Academy of Sciences, vol.83, pp.2531-2535, 1986.

B. B. Minkoff, S. Makino, M. Haruta, E. T. Beebe, R. L. Wrobel et al., A cell-free method for expressing and reconstituting membrane proteins enables functional characterization of the plant receptor-like protein kinase FERONIA, Journal of Biological Chemistry, vol.292, pp.5932-5942, 2017.

M. Minor and B. Slagle, Hepatitis B Virus HBx Protein Interactions with the Ubiquitin Proteasome System, Viruses, vol.6, pp.4683-4702, 2014.

K. Miura, M. Tachibana, E. Takashima, M. Morita, B. N. Kanoi et al., Malaria transmission-blocking vaccines: wheat germ cell-free technology can accelerate vaccine development, Expert Rev. Vaccines, 2019.

G. Moraleda, T. Wu, A. R. Jilbert, C. E. Aldrich, L. D. Condreay et al., Inhibition of duck hepatitis B virus replication by hypericin, Antiviral Research, vol.20, pp.235-247, 1993.

E. H. Morita, M. Shimizu, T. Ogasawara, Y. Endo, R. Tanaka et al., A novel way of amino acid-specific assignment in 1 H-15 N HSQC spectra with a wheat germ cell-free protein synthesis system, Journal of Biomolecular NMR, vol.30, pp.37-45, 2004.

D. C. Muchmore, L. P. Mcintosh, C. B. Russell, D. E. Anderson, and F. W. Dahlquist, Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance, Methods in Enzymology, pp.77005-77006, 1989.

H. Mueller, A. Lopez, P. Tropberger, S. Wildum, J. Schmaler et al., PAPD5/7 Are Host Factors That Are Required for Hepatitis B Virus RNA Stabilization, Hepatology, vol.69, pp.1398-1411, 2019.

H. Mueller, S. Wildum, S. Luangsay, J. Walther, A. Lopez et al., A novel orally available small molecule that inhibits hepatitis B virus expression, Journal of Hepatology, vol.68, pp.412-420, 2018.

A. Mukherji, V. C. Janbandhu, and V. Kumar, HBx-dependent cell cycle deregulation involves interaction with cyclin E/A-cdk2 complex and destabilization of p27 Kip1, Biochem. J, vol.401, pp.247-256, 2007.

S. Murakami, J. H. Cheong, and S. Kaneko, Human hepatitis virus X gene encodes a regulatory domain that represses transactivation of X protein, J Biol Chem, vol.269, pp.15118-15123, 1994.

M. Myshkin, . Yu, R. Männikkö, O. A. Krumkacheva, D. S. Kulbatskii et al., Cell-Free Expression of Sodium Channel Domains for Pharmacology Studies. Noncanonical Spider Toxin Binding Site in the Second Voltage-Sensing Domain of Human Nav1.4 Channel, Front. Pharmacol, vol.10, p.953, 2019.

M. Nassal, Hepatitis B viruses: Reverse transcription a different way, Virus Research, vol.134, pp.235-249, 2008.

M. Nassal, HBV cccDNA: viral persistence reservoir and key obstacle for a cure of chronic hepatitis B, Gut, vol.64, pp.1972-1984, 2015.

M. Nassal and A. Rieger, An Intramolecular Disulfide Bridge between Cys-7 and Cys6l Determines the Structure of the Secretory Core Gene Product (e Antigen) of Hepatitis B Virus, Journal of Virology, vol.67, pp.4307-4315, 1993.

K. Nemoto, T. Seto, H. Takahashi, A. Nozawa, M. Seki et al., Autophosphorylation profiling of Arabidopsis protein kinases using the cell-free system, Phytochemistry, vol.72, pp.1136-1144, 2011.

A. R. Neurath, S. B. Kent, N. Strick, and K. Parker, Identification and chemical synthesis of a host cell receptor binding site on hepatitis B virus, Cell, vol.46, issue.86, p.90663, 1986.

D. E. Nevin and J. M. Pratt, A coupled in vitro transcription-translation system for the exclusive synthesis of polypeptides expressed from the T7 promoter, FEBS Letters, vol.291, pp.259-263, 1991.

Y. Ni, F. A. Lempp, S. Mehrle, S. Nkongolo, C. Kaufman et al., Hepatitis B and D Viruses Exploit Sodium Taurocholate Co-transporting Polypeptide for Species-Specific Entry into Hepatocytes, Gastroenterology, vol.146, pp.1070-1083, 2014.

A. Nicoll, S. Locarnini, S. T. Chou, R. Smallwood, A. et al., Effect of nucleoside analogue therapy on duck hepatitis B viral replication in hepatocytes and bile duct epithelial cells in vivo, Journal of Gastroenterology and Hepatology, vol.15, pp.304-310, 2000.

J. T. Nielsen, M. Bjerring, M. D. Jeppesen, R. O. Pedersen, J. M. Pedersen et al., Unique Identification of Supramolecular Structures in Amyloid Fibrils by Solid-State NMR Spectroscopy, Angew. Chem. Int. Ed, vol.48, pp.2118-2121, 2009.

A. J. Nieuwkoop and C. M. Rienstra, Supramolecular Protein Structure Determination by Site-Specific Long-Range Intermolecular Solid State NMR Spectroscopy, J. Am. Chem. Soc, vol.132, pp.7570-7571, 2010.

X. Ning, S. H. Basagoudanavar, K. Liu, L. Luckenbaugh, D. Wei et al., Capsid Phosphorylation State and Hepadnavirus Virion Secretion, Journal of Virology, vol.91, pp.92-109, 2017.

X. Ning, L. Luckenbaugh, K. Liu, V. Bruss, C. Sureau et al., Common and Distinct Capsid and Surface Protein Requirements for Secretion of Complete and Genome-Free Hepatitis B Virions, J Virol, vol.92, pp.272-290, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02370844

X. Ning, D. Nguyen, L. Mentzer, C. Adams, H. Lee et al., Secretion of Genome-Free Hepatitis B Virus -Single Strand Blocking Model for Virion Morphogenesis of Para-retrovirus, PLoS Pathogens, vol.7, 2011.

M. W. Nirenberg and J. H. Matthaei, The dependence of cell-free protein synthesis in E. coli upon naturally occurring or synthetic polyribonucleotides, Proc Natl Acad Sci U S A, vol.47, pp.1588-1602, 1961.

C. Noirot, B. Habenstein, L. Bousset, R. Melki, B. H. Meier et al., Wheat-germ cell-free production of prion proteins for solid-state NMR structural studies, New Biotechnology, vol.28, pp.232-238, 2011.
URL : https://hal.archives-ouvertes.fr/hal-01183181

S. M. Nomura, S. Kondoh, W. Asayama, A. Asada, S. Nishikawa et al., Direct preparation of giant proteo-liposomes by in vitro membrane protein synthesis, Journal of Biotechnology, vol.133, pp.190-195, 2008.

F. Noordeen, C. A. Scougall, A. Grosse, Q. Qiao, B. B. Ajilian et al., Therapeutic Antiviral Effect of the Nucleic Acid Polymer REP 2055 against Persistent Duck Hepatitis B Virus Infection, PLoS ONE, vol.10, 2015.

I. V. Novikova, N. Sharma, T. Moser, R. Sontag, Y. Liu et al., Protein structural biology using cellfree platform from wheat germ, Advanced Structural and Chemical Imaging, vol.4, p.13, 2018.

A. Nozawa and Y. Tozawa, Modifications of Wheat Germ Cell-Free System for Functional Proteomics of Plant Membrane Proteins, pp.259-272, 2014.

A. Nozawa, H. Nanamiya, T. Miyata, N. Linka, Y. Endo et al., A Cell-Free Translation and Proteoliposome Reconstitution System for Functional Analysis of Plant Solute Transporters, Plant and Cell Physiology, vol.48, pp.1815-1820, 2007.

A. P. O'connell, M. K. Urban, and W. T. London, Naturally occurring infection of Pekin duck embryos by duck hepatitis B virus, Proceedings of the National Academy of Sciences, vol.80, pp.1703-1706, 1983.

S. Obert, B. Zachmann-brand, E. Deindl, W. Tucker, R. Bartenschlager et al., A spliced hepadnavirus RNA that is essential for virus replication, The EMBO Journal, vol.15, pp.2565-2574, 1996.

T. Ogasawara, T. Sawasaki, R. Morishita, A. Ozawa, K. Madin et al., A new class of enzyme acting on damaged ribosomes: ribosomal RNA apurinic site specific lyase found in wheat germ, EMBO J, vol.18, pp.6522-6531, 1999.

T. Ohlmann, M. Rau, S. J. Morley, and V. M. Pain, , 1995.

C. L. Olliuer and C. D. Boyd, In Vitro Translation of Messenger RNA in a Rabbit Reticulocyte, vol.11

S. K. Ono, N. Kato, Y. Shiratori, J. Kato, T. Goto et al., The polymerase L528M mutation cooperates with nucleotide binding-site mutations, increasing hepatitis B virus replication and drug resistance, J. Clin. Invest, vol.107, pp.449-455, 2001.

M. L. Op-den-brouw, R. S. Binda, M. H. Van-roosmalen, U. Protzer, H. L. Janssen et al., , 2009.

, Hepatitis B virus surface antigen impairs myeloid dendritic cell function: a possible immune escape mechanism of hepatitis B virus, Immunology, vol.126, pp.280-289

J. S. Opella, The development of solid-state NMR of membrane proteins, Biomedical Spectroscopy and Imaging, pp.81-105, 2014.

S. J. Opella, M. H. Frey, and T. A. Cross, Detection of individual carbon resonances in solid proteins, J. Am. Chem. Soc, vol.101, pp.5856-5857, 1979.

P. Ostapchuk, P. Hearing, and D. Ganem, , 1994.

G. Radziwill, W. Tucker, and H. Schaller, Mutational Analysis of the Hepatitis B Virus P Gene Product: Domain Structure and RNase H Activity, Journal of Virology, vol.64, pp.613-620, 1990.

Z. Rahmani, K. Huh, R. Lasher, and A. Siddiqui, Hepatitis B Virus X Protein Colocalizes to Mitochondria with a Human Voltage-Dependent Anion Channel, HVDAC3, and Alters Its Transmembrane Potential, Journal of Virology, vol.74, pp.2840-2846, 2000.

A. M. Rakotondrafara and M. W. Hentze, An efficient factor-depleted mammalian in vitro translation system, Nat Protoc, vol.6, pp.563-571, 2011.

D. Ramakrishnan, W. Xing, R. K. Beran, S. Chemuru, H. Rohrs et al., Hepatitis B Virus X Protein Function Requires Zinc Binding, J Virol, vol.93, pp.250-269, 2019.

R. M. Rasia, B. Brutscher, and M. J. Plevin, Selective Isotopic Unlabeling of Proteins Using Metabolic Precursors: Application to NMR Assignment of Intrinsically Disordered Proteins, ChemBioChem, vol.13, pp.732-739, 2012.

T. Ravula, N. Z. Hardin, and A. Ramamoorthy, Polymer nanodiscs: Advantages and limitations, Chem. Phys. Lipids, vol.219, pp.45-49, 2019.

J. S. Rawlings, The JAK/STAT signaling pathway, Journal of Cell Science, vol.117, pp.1281-1283, 2004.

, PDB Statistics: Growth of Structures from NMR Experiments Released per Year, RCSB Protein Data Bank, 2019.

B. Rehermann, C. Ferrari, C. Pasquinelli, and F. V. Chisari, The hepatitis B virus persists for decades after patients' recovery from acute viral hepatitis despite active maintenance of a cytotoxic T-lymphocyte response, Nat Med, vol.2, pp.1104-1108, 1996.

J. S. Retel, A. J. Nieuwkoop, M. Hiller, V. A. Higman, E. Barbet-massin et al., Structure of outer membrane protein G in lipid bilayers, Nature Communications, vol.8, p.2073, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01679641

P. Revill, L. Yuen, R. Walsh, M. Perrault, S. Locarnini et al., Bioinformatic analysis of the hepadnavirus e-antigen and its precursor identifies remarkable sequence conservation in all orthohepadnaviruses, J. Med. Virol, vol.82, pp.104-115, 2010.

S. Ritz, M. Hulko, C. Zerfass, S. May, I. Hospach et al., Cell-free expression of a mammalian olfactory receptor and unidirectional insertion into small unilamellar vesicles (SUVs), Biochimie, vol.95, pp.1909-1916, 2013.

B. E. Roberts and B. M. Paterson, Efficient Translation of Tobacco Mosaic Virus RNA and Rabbit Globin 9S RNA in a Cell-Free System from Commercial Wheat Germ, Proceedings of the National Academy of Sciences, vol.70, pp.2330-2334, 1973.

W. S. Robinson and R. L. Greenman, DNA Polymerase in the Core of the Human Hepatitis B Virus Candidate, vol.13, p.6, 1974.

M. J. Roossinck, S. Jameel, S. H. Loukin, and A. Siddiqui, Expression of hepatitis B viral core region in mammalian cells, Mol. Cell. Biol, vol.6, pp.1393-1400, 1986.

A. M. Roseman, J. A. Berriman, S. A. Wynne, P. J. Butler, and R. A. Crowther, A structural model for maturation of the hepatitis B virus core, Proceedings of the National Academy of Sciences, vol.102, pp.15821-15826, 2005.

K. Rothmann, M. S. Lzer, G. Radziwill, E. Hildt, K. Moelling et al., Host Cell-Virus Cross Talk: Phosphorylation of a Hepatitis B Virus Envelope Protein Mediates Intracellular Signaling, Journal of Virology, vol.72, p.10, 1998.

H. M. Rothnie, Y. Chapdelaine, and T. Hohn, Pararetroviruses and retroviruses: a comparative review of viral structure and gene expression strategies, Adv Virus Res, vol.44, pp.1-67, 1994.

S. Ruehrer and H. Michel, Exploiting Leishmania tarentolae cell-free extracts for the synthesis of human solute carriers, Molecular Membrane Biology, vol.30, pp.288-302, 2013.

G. E. Rydell, K. Prakash, H. Norder, and M. Lindh, Hepatitis B surface antigen on subviral particles reduces the neutralizing effect of anti-HBs antibodies on hepatitis B viral particles in vitro, Virology, vol.509, pp.67-70, 2017.

R. Sachse, S. K. Dondapati, S. F. Fenz, T. Schmidt, and S. Kubick, Membrane protein synthesis in cell-free systems: From bio-mimetic systems to bio-membranes, FEBS Letters, vol.588, pp.2774-2781, 2014.

A. S. Salehi, M. T. Smith, A. M. Bennett, J. B. Williams, W. G. Pitt et al., Cell-free protein synthesis of a cytotoxic cancer therapeutic: Onconase production and a just-add-water cell-free system, Biotechnology Journal, vol.11, pp.274-281, 2016.

J. Salisse and C. Sureau, A Function Essential to Viral Entry Underlies the Hepatitis B Virus "a" Determinant, Journal of Virology, vol.83, pp.9321-9328, 2009.

R. Sanjuán, From Molecular Genetics to Phylodynamics: Evolutionary Relevance of Mutation Rates Across Viruses, PLoS Pathog, vol.8, p.1002685, 2012.

S. Sarrazin, W. C. Lamanna, and J. D. Esko, Heparan Sulfate Proteoglycans, Cold Spring Harbor Perspectives in Biology, vol.3, pp.4952-004952, 2011.

W. Saso, S. Tsukuda, H. Ohashi, K. Fukano, R. Morishita et al., A new strategy to identify hepatitis B virus entry inhibitors by AlphaScreen technology targeting the envelope-receptor interaction, Biochemical and Biophysical Research Communications, vol.501, pp.374-379, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02370847

O. Satoh, H. Imai, T. Yoneyama, T. Miyamura, H. Utsumi et al., Membrane structure of the hepatitis B virus surface antigen particle, J. Biochem, vol.127, pp.543-550, 2000.

O. Satoh, M. Umeda, H. Imai, H. Tunoo, and K. Inoue, Lipid composition of hepatitis B virus surface antigen particles and the particle-producing human hepatoma cell lines, Journal of Lipid Research, vol.31, pp.1293-1300, 1990.

M. Saunders, A. Wishnia, and J. G. Kirkwood, The Nuclear Magnetic Resonance Spectrum of Ribonuclease 1, J. Am. Chem. Soc, vol.79, pp.3289-3290, 1957.

O. Saurel, I. O. Iordanov, G. Nars, P. Demange, T. L. Marchand et al., Local and global dynamics in Klebsiella pneumoniae outer membrane protein A in lipid bilayers probed at atomic resolution, Journal of the American Chemical Society, vol.139, pp.1590-1597, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01503512

T. Sawasaki, Y. Hasegawa, M. Tsuchimochi, N. Kamura, T. Ogasawara et al., A bilayer cell-free protein synthesis system for high-throughput screening of gene products, FEBS Lett, vol.514, pp.102-105, 2002.

L. Sborgi, F. Ravotti, V. P. Dandey, M. S. Dick, A. Mazur et al., Structure and assembly of the mouse ASC inflammasome by combined NMR spectroscopy and cryo-electron microscopy, Proceedings of the National Academy of Sciences, vol.112, pp.13237-13242, 2015.

G. Scheele and P. Blackburn, Role of mammalian RNase inhibitor in cell-free protein synthesis, Proceedings of the National Academy of Sciences, vol.76, pp.4898-4902, 1979.

A. Schmitz, A. Schwarz, M. Foss, L. Zhou, B. Rabe et al., Nucleoporin 153 Arrests the Nuclear Import of Hepatitis B Virus Capsids in the Nuclear Basket, PLoS Pathog, vol.6, 2010.
URL : https://hal.archives-ouvertes.fr/hal-00522959

J. A. Schoborg, J. M. Hershewe, J. C. Stark, W. Kightlinger, J. E. Kath et al., A cell-free platform for rapid synthesis and testing of active oligosaccharyltransferases, Biotechnol. Bioeng, vol.115, pp.739-750, 2018.

F. Schodel, D. Peterson, J. Zheng, J. E. Jones, J. L. Hughes et al., Structure of hepatitis B virus core and e-antigen. A single precore amino acid prevents nucleocapsid assembly, J Biol Chem, vol.268, pp.1332-1337, 1993.

U. Schultz, E. Grgacic, and M. Nassal, Duck Hepatitis B Virus: An Invaluable Model System for HBV Infection, Advances in Virus Research, pp.63001-63007, 2004.

A. Schulze, P. Gripon, and S. Urban, Hepatitis B virus infection initiates with a large surface protein-dependent binding to heparan sulfate proteoglycans, Hepatology, vol.46, p.10, 2007.
URL : https://hal.archives-ouvertes.fr/hal-00690474

A. Schulze, A. Schieck, Y. Ni, W. Mier, and S. Urban, Fine Mapping of Pre-S Sequence Requirements for Hepatitis B Virus Large Envelope Protein-Mediated Receptor Interaction, Journal of Virology, vol.84, 1989.

A. K. Schütz, B. Habenstein, N. Luckgei, L. Bousset, Y. Sourigues et al., Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p, Biomol NMR Assign, vol.8, pp.349-356, 2014.

H. Schwalbe, Editorial: New 1.2 GHz NMR Spectrometers-New Horizons?, Angew Chem Int Ed Engl, vol.56, pp.10252-10253, 2017.

D. Schwarz, D. Daley, T. Beckhaus, V. Dötsch, B. et al., Cell-free expression profiling of E. coli inner membrane proteins, Proteomics, vol.10, pp.1762-1779, 2010.

D. Schwarz, V. Dötsch, B. , and F. , Production of membrane proteins using cell-free expression systems, Proteomics, vol.8, pp.3933-3946, 2008.

R. Schweet, H. Lamfrom, A. , and E. , The Synthesis of Hemoglobin in a Cell-Free System, Biochemistry, vol.44, p.7, 1958.

A. Schweitzer, J. Horn, R. T. Mikolajczyk, G. Krause, and J. J. Ott, Estimations of worldwide prevalence of chronic hepatitis B virus infection: a systematic review of data published between, The Lancet, vol.386, p.61412, 1965.

E. J. Scourfield and J. Martin-serrano, Growing functions of the ESCRT machinery in cell biology and viral replication, Biochm. Soc. Trans, vol.45, pp.613-634, 2017.

A. M. Seddon, P. Curnow, and P. J. Booth, Membrane proteins, lipids and detergents: not just a soap opera, Biochimica et Biophysica Acta (BBA) -Biomembranes, vol.1666, pp.105-117, 2004.

C. Seeger and W. S. Mason, Molecular biology of hepatitis B virus infection. Virology 479-480, 672-686, 2015.

C. Seeger and J. A. Sohn, Targeting Hepatitis B Virus With CRISPR/Cas9. Molecular Therapy -Nucleic Acids, p.7, 2014.

C. Seeger, F. Zoulim, and W. S. Mason, Hepadnavirus," in Fields Virology, pp.2185-2221, 2013.

S. Seitz, C. Iancu, T. Volz, W. Mier, M. Dandri et al., A Slow Maturation Process Renders Hepatitis B Virus Infectious, Cell Host & Microbe, vol.20, pp.25-35, 2016.

S. Seitz, S. Urban, C. Antoni, and B. Böttcher, Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions, The EMBO Journal, vol.26, pp.4160-4167, 2007.

E. Seki, T. Yanagisawa, Y. , and S. , Cell-Free Protein Synthesis for Multiple Site-Specific Incorporation of Noncanonical Amino Acids Using Cell Extracts from RF-1 Deletion E. coli Strains, Methods Mol Biol, vol.1728, pp.49-65, 2018.

L. Selzer, S. P. Katen, and A. Zlotnick, The Hepatitis B Virus Core Protein Intradimer Interface Modulates Capsid Assembly and Stability, Biochemistry, vol.53, pp.5496-5504, 2014.

N. Sen, F. Cao, and J. E. Tavis, Translation of Duck Hepatitis B Virus Reverse Transcriptase by Ribosomal Shunting, Journal of Virology, vol.78, pp.11751-11757, 2004.

S. A. Shahid, B. Bardiaux, W. T. Franks, L. Krabben, M. Habeck et al., Membrane-protein structure determination by solid-state NMR spectroscopy of microcrystals, Nat Methods, vol.9, pp.1212-1217, 2012.

M. Shally, N. Alloul, A. Jackman, M. Muller, L. Gissmann et al., The E6 variant proteins E6I-E6IV of human papillomavirus 16: expression in cell free systems and bacteria and study of their interaction with p53, Virus Research, vol.42, pp.81-96, 1996.

M. Sharma, M. Yi, H. Dong, H. Qin, E. Peterson et al., Insight into the Mechanism of the Influenza A Proton Channel from a Structure in a Lipid Bilayer, Science, vol.330, pp.509-512, 2010.

F. Shen, Y. Li, Y. Wang, V. Sozzi, P. A. Revill et al., Hepatitis B virus sensitivity to interferon-? in hepatocytes is more associated with cellular interferon response than with viral genotype, Hepatology, vol.67, pp.1237-1252, 2018.

J. Shi, J. G. Pelton, H. S. Cho, and D. E. Wemmer, Protein Signal Assignments Using Specific Labeling and Cell-Free Synthesis, Journal of Biomolecular NMR, vol.28, pp.235-247, 2003.

Y. Shimizu, A. Inoue, Y. Tomari, T. Suzuki, T. Yokogawa et al., Cell-free translation reconstituted with purified components, Nat Biotechnol, vol.19, pp.751-755, 2001.

S. Shimura, K. Watashi, K. Fukano, M. Peel, A. Sluder et al., Cyclosporin derivatives inhibit hepatitis B virus entry without interfering with NTCP transporter activity, Journal of Hepatology, vol.66, pp.685-692, 2017.

Y. Shin, C. Ko, and W. Ryu, Hydrophobic residues of terminal protein domain of hepatitis B virus polymerase contribute to distinct steps in viral genome replication, FEBS Letters, vol.585, pp.3964-3968, 2011.

Y. Shin, S. Park, and W. Ryu, A conserved arginine residue in the terminal protein domain of hepatitis B virus polymerase is critical for RNA pre-genome encapsidation, J Gen Virol, vol.92, pp.1809-1816, 2011.

T. Shinoda, N. Shinya, K. Ito, Y. Ishizuka-katsura, N. Ohsawa et al., Cell-free methods to produce structurally intact mammalian membrane proteins, Scientific Reports, vol.6, p.30442, 2016.

J. M. Short, S. Chen, A. M. Roseman, P. J. Butler, and R. A. Crowther, Structure of Hepatitis B Surface Antigen from Subviral Tubes Determined by Electron Cryomicroscopy, Journal of Molecular Biology, vol.390, pp.135-141, 2009.

D. Shouval, Hepatitis B vaccines, Journal of Hepatology, vol.39, pp.70-76, 2003.

K. Sidhu, S. Kumar, V. S. Reddy, and V. Kumar, Mass Spectrometric Determination of Disulfide Bonds in the Biologically Active Recombinant HBx Protein of Hepatitis B Virus, Biochemistry, vol.53, pp.4685-4695, 2014.

V. D. Siegler and V. Bruss, Role of Transmembrane Domains of Hepatitis B Virus Small Surface Proteins in Subviral-Particle Biogenesis, Journal of Virology, vol.87, pp.1491-1496, 2013.

L. O. Sillerud and R. S. Larson, Advances in Nuclear Magnetic Resonance for Drug Discovery, Bioinformatics and Drug Discovery, pp.195-266, 2012.

P. Simmonds, The origin and evolution of hepatitis viruses in humans, J Gen Virol, vol.82, pp.693-712, 2001.

B. L. Slagle and M. J. Bouchard, Hepatitis B Virus X and Regulation of Viral Gene Expression. Cold Spring Harb Perspect Med 6, a021402, 2016.

S. K. Smailov, A. V. Lee, and B. K. Iskakov, Study of phosphorylation of translation elongation factor 2 (EF-2) from wheat germ, FEBS Letters, vol.321, issue.93, pp.80112-80120, 1993.

I. Smith, G. Donello, J. E. Lück, R. Steger, G. Hope et al., The hepatitis B virus post-transcriptional regulatory element contains two conserved RNA stem-loops which are required for function, Nucleic Acids Research, vol.26, pp.4818-4827, 1998.

G. E. Smith, M. D. Summers, and M. J. Fraser, Production of human beta interferon in insect cells infected with a baculovirus expression vector, Molecular and Cellular Biology, vol.3, pp.2156-2165, 1983.

S. Smith-penzel, Solid-state NMR under fast magic-angle spinning (90-150 kHz) for biological applications, 2018.

M. Somiya, Y. Sasaki, T. Matsuzaki, Q. Liu, M. Iijima et al., Intracellular trafficking of bionanocapsule-liposome complex: Identification of fusogenic activity in the pre-S1 region of hepatitis B virus surface antigen L protein, Journal of Controlled Release, vol.212, pp.10-18, 2015.

N. Sonveaux, D. Thines, and J. M. Ruysschaert, Characterization of the HBsAg particle lipid membrane, Research in Virology, vol.146, pp.43-51, 1995.

A. Spirin, V. Baranov, L. Ryabova, S. Ovodov, A. et al., A continuous cell-free translation system capable of producing polypeptides in high yield, Science, vol.242, pp.1162-1164, 1988.

R. Sprengel, C. Kuhn, H. Will, and H. Schaller, Comparative sequence analysis of duck and human hepatitis B virus genomes, J. Med. Virol, vol.15, pp.323-333, 1985.

N. C. Srivastav, N. Shakya, M. Mak, B. Agrawal, D. L. Tyrrell et al., Antiviral Activity of Various 1-(2?-Deoxy-?-D -lyxofuranosyl), 1-(2?-Fluoro-?-D -xylofuranosyl), 1-(3?-Fluoro-?-D -arabinofuranosyl), and 2?-Fluoro-2?,3?-didehydro-2?,3?-dideoxyribose Pyrimidine Nucleoside Analogues against Duck Hepatitis B Virus (DHBV) and Human Hepatitis B Virus (HBV) Replication, Journal of Medicinal Chemistry, vol.53, pp.7156-7166, 2010.

M. Stahl, J. Beck, and M. Nassal, Chaperones Activate Hepadnavirus Reverse Transcriptase by Transiently Exposing a C-Proximal Region in the Terminal Protein Domain That Contributes to RNA Binding, Journal of Virology, vol.81, pp.13354-13364, 2007.

L. F. Stancato, K. A. Hutchison, P. Krishna, and W. B. Pratt, Animal and Plant Cell Lysates Share a Conserved Chaperone System That Assembles the Glucocorticoid Receptor into a Functional Heterocomplex with hsp90 ?, Biochemistry, vol.35, pp.554-561, 1996.

J. Stephenne, Recombinant versus plasma-derived hepatitis B vaccines: issues of safety, immunogenicity and costeffectiveness, Vaccine, vol.6, pp.90173-90182, 1988.

J. Stephenne, Development and production aspects of a recombinant yeast-derived hepatitis B vaccine, Vaccine, vol.8, pp.69-73, 1990.

J. T. Stieler and R. Prange, Involvement of ESCRT-II in Hepatitis B Virus Morphogenesis, PLoS ONE, vol.9, p.91279, 2014.

H. J. Stirk, J. M. Thornton, and C. R. Howard, A topological model for hepatitis B surface antigen, Intervirology, vol.33, pp.148-158, 1992.

L. Stoeckl, A. Funk, A. Kopitzki, B. Brandenburg, S. Oess et al., Identification of a structural motif crucial for infectivity of hepatitis B viruses, Proceedings of the National Academy of Sciences, vol.103, pp.6730-6734, 2006.

S. J. Stray, P. Ceres, and A. Zlotnick, Zinc Ions Trigger Conformational Change and Oligomerization of Hepatitis B Virus Capsid Protein ?, Biochemistry, vol.43, pp.9989-9998, 2004.

C. S. Su, S. Bowden, L. P. Fong, and H. R. Taylor, Detection of hepatitis B virus DNA in tears by polymerase chain reaction, Arch Ophthalmol, vol.112, pp.621-625, 1994.

X. Su, C. Loh, R. Qi, and G. Otting, Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O, Journal of Biomolecular NMR, vol.50, pp.35-42, 2011.

S. Suffner, N. Gerstenberg, M. Patra, P. Ruibal, A. Orabi et al., Domains of the Hepatitis B Virus Small Surface Protein S Mediating Oligomerization, Journal of Virology, vol.92, pp.2232-2249, 2018.

A. Suh, C. C. Weber, C. Kehlmaier, E. L. Braun, R. E. Green et al., Early Mesozoic Coexistence of Amniotes and Hepadnaviridae, PLoS Genet, vol.10, 2014.

J. Summers, Three recently described animal virus models for human hepatitis B virus, Hepatology, vol.1, pp.179-183, 1981.

J. Summers, A. O'connell, and I. Millman, Genome of hepatitis B virus: restriction enzyme cleavage and structure of DNA extracted from Dane particles, Proceedings of the National Academy of Sciences, vol.72, pp.4597-4601, 1975.

J. Summers, P. M. Smith, M. Huang, Y. , and M. , Morphogenetic and Regulatory Effects of Mutations in the Envelope Proteins of an Avian Hepadnavirus, Journal of Virology, vol.65, 1991.

J. Summers, J. M. Smolec, and R. Snyder, A virus similar to human hepatitis B virus associated with hepatitis and hepatoma in woodchucks, Proceedings of the National Academy of Sciences, vol.75, pp.4533-4537, 1978.

X. Sun, H. J. Dyson, and P. E. Wright, Kinetic analysis of the multistep aggregation pathway of human transthyretin, 2018.

, Proc Natl Acad Sci USA, vol.115

J. J. Sung, K. K. Tsoi, V. W. Wong, K. C. Li, C. et al., Meta-analysis: treatment of hepatitis B infection reduces risk of hepatocellular carcinoma, Alimentary Pharmacology & Therapeutics, vol.28, pp.1067-1077, 2008.

C. Sureau and J. Salisse, A conformational heparan sulfate binding site essential to infectivity overlaps with the conserved hepatitis B virus A-determinant, Hepatology, vol.57, pp.985-994, 2013.

R. Wang, Y. Iwakura, K. Araki, H. Sotoyama, N. Takei et al., In vitro production of an active neurotrophic factor, neuregulin-1: Qualitative comparison of different cell-free translation systems, Neuroscience Letters, vol.497, pp.90-93, 2011.

S. Wang, M. Fogeron, M. Schledorn, M. Dujardin, S. Penzel et al., Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation, Front. Mol. Biosci, vol.6, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02322693

S. Wang, R. A. Munro, L. Shi, I. Kawamura, T. Okitsu et al., Solid-state NMR spectroscopy structure determination of a lipid-embedded heptahelical membrane protein, Nat Methods, vol.10, pp.1007-1012, 2013.

Z. Wang, S. Gao, X. Li, F. Sun, F. Li et al., , 2015.

M. E. Ward, S. Wang, R. Munro, E. Ritz, I. Hung et al., Situ Structural Studies of Anabaena Sensory, vol.108, pp.1683-1696, 2015.

G. Waris, K. Huh, and A. Siddiqui, Mitochondrially Associated Hepatitis B Virus X Protein Constitutively Activates Transcription Factors STAT-3 and NF-B via Oxidative Stress, MOL. CELL. BIOL, vol.21, p.10, 2001.

N. Warner and S. Locarnini, Mechanisms of Hepatitis B Virus Resistance Development, Intervirology, vol.57, pp.218-224, 2014.

G. Wasenauer, J. Kock, and H. Schlicht, A Cysteine and a Hydrophobic Sequence in the Noncleaved Portion of the Pre-C Leader Peptide Determine the Biophysical Properties of the Secretory Core Protein (HBe Protein) of Human Hepatitis B Virus, Journal of Virology, vol.66, pp.5338-5346, 1992.

M. Watanabe, K. Miyazono, M. Tanokura, T. Sawasaki, Y. Endo et al., Cell-free protein synthesis for structure determination by X-ray crystallography, Methods Mol Biol, vol.607, pp.149-160, 2010.

E. D. Watt and C. M. Rienstra, Recent Advances in Solid-State Nuclear Magnetic Resonance Techniques to Quantify Biomolecular Dynamics, Anal. Chem, vol.86, pp.58-64, 2014.

A. Watts, Nuclear magnetic resonance methods to characterize lipid-protein interactions at membrane surfaces, J Bioenerg Biomembr, vol.19, pp.625-653, 1987.

N. R. Watts, J. F. Conway, N. Cheng, S. J. Stahl, D. M. Belnap et al., , 2002.

N. R. Watts, J. F. Conway, N. Cheng, S. J. Stahl, A. C. Steven et al., Role of the Propeptide in Controlling Conformation and Assembly State of Hepatitis B Virus e-Antigen, Journal of Molecular Biology, vol.409, pp.202-213, 2011.

N. R. Watts, J. G. Vethanayagam, R. B. Ferns, R. S. Tedder, A. Harris et al., Molecular Basis for the High Degree of Antigenic Cross-Reactivity between Hepatitis B Virus Capsids (HBcAg) and Dimeric Capsid-Related Protein (HBeAg): Insights into the Enigmatic Nature of the e-Antigen, Journal of Molecular Biology, vol.398, pp.530-541, 2010.

L. A. Weber, E. R. Feman, and C. Baglioni, A Cell Free System from HeLa Cells Active in Initiation of Protein Synthesis, Biochemistry, vol.14, pp.5315-5321, 1975.

M. Weber, V. Bronsema, H. Bartos, A. Bosserhoff, R. Bartenschlager et al., , 1994.

, Hepadnavirus P Protein Utilizes a Tyrosine Residue in the TP Domain To Prime Reverse Transcription, Journal of Virology, vol.68, pp.2994-2999

X. Wei and D. L. Peterson, Expression, Purification, and Characterization of an Active RNase H Domain of the Hepatitis B Viral Polymerase, J. Biol. Chem, vol.271, pp.32617-32622, 1996.

Y. Wei, J. E. Tavis, and D. Ganem, Relationship between Viral DNA Synthesis and Virion Envelopment in Hepatitis B Viruses, Journal of Virology, vol.70, pp.6455-6458, 1996.

B. Werle-lapostolle, S. Bowden, S. Locarnini, K. Wursthorn, J. Petersen et al., Persistence of cccDNA during the natural history of chronic hepatitis B and decline during adefovir dipivoxil therapy1, Gastroenterology, vol.126, pp.1750-1758, 2004.

M. Werr and R. Prange, Role for Calnexin and N-Linked Glycosylation in the Assembly and Secretion of Hepatitis B Virus Middle Envelope Protein Particles, Journal of Virology, vol.72, 1998.

M. Widmann, C. , and P. , Comparison of Folding Rates of Homologous Prokaryotic and Eukaryotic Proteins, J. Biol. Chem, vol.275, pp.18619-18622, 2000.

T. Wiegand, R. Cadalbert, D. Lacabanne, J. Timmins, L. Terradot et al., The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase, Nat Commun, vol.10, p.31, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02322585

T. Wiegand, D. Lacabanne, K. Keller, R. Cadalbert, L. Lecoq et al., Solid-state NMR and EPR Spectroscopy of Mn 2+ -Substituted ATP-Fueled Protein Engines, Angew. Chem. Int. Ed, vol.56, pp.3369-3373, 2017.

M. P. Williamson, T. F. Have, and K. Wiithrich, Solution Conformation of Proteinase Inhibitor IIA from Bull Seminal Plasma by 'H Nuclear Magnetic Resonance and Distance Geometry, J. Mol. Biol, vol.182, pp.295-315, 1985.

T. M. Wilson, R. N. Perham, and P. J. Butler, Intermediates in the disassembly of tobacco mosaic virus at alkaline pH Infectivity, self-assembly, and translational activities, Virology, vol.89, pp.475-483, 1978.

P. T. Wingfield, S. J. Stahl, R. W. Williams, and A. C. Steven, Hepatitis Core Antigen Produced in Escherichia coli: Subunit Composition, Conformational Analysis, and In Vitro Capsid Assemblyt, Biochemistry, vol.34, pp.4919-4932, 1995.

K. Wisskirchen, J. Kah, A. Malo, T. Asen, T. Volz et al., T cell receptor grafting allows virological control of hepatitis B virus infection, Journal of Clinical Investigation, vol.129, pp.2932-2945, 2019.

, Hepatitis B. World Health Organization, World Health Organization, 2019.

, WHO UNICEF coverage estimates WHO World Health Organization: Immunization, Vaccines And Biologicals. Vaccine preventable diseases Vaccines monitoring system, Global Summary Reference Time Series: DTP3. WHO-UNICEF estimates of DTP3 coverage. Available at, 2019.

A. Woznicka-misaila, C. Juillan-binard, D. Baud, E. Pebay-peyroula, and S. Ravaud, Cell-free production, purification and characterization of human mitochondrial ADP/ATP carriers, Protein Expression and Purification, vol.144, pp.46-54, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01685067

P. S. Wu, K. Ozawa, S. Jergic, X. Su, N. E. Dixon et al., Amino-acid Type Identification in 15N-HSQC Spectra by Combinatorial Selective 15N-labelling, J. Biomol. NMR, vol.34, pp.13-21, 2006.

G. Wunderlich and V. Bruss, Characterization of early hepatitis B virus surface protein oligomers, Archives of Virology, vol.141, pp.1191-1205, 1996.

K. Wüthrich, NMR studies of structure and function of biological macromolecules (Nobel Lecture), Journal of Biomolecular NMR, p.28, 2003.

S. A. Wynne, R. A. Crowther, and A. G. Leslie, The Crystal Structure of the Human Hepatitis B Virus Capsid, Molecular Cell, vol.3, pp.771-780, 1999.

Y. Xu, J. Lee, C. Tran, T. H. Heibeck, W. D. Wang et al., Production of bispecific antibodies in "knobsinto-holes" using a cell-free expression system, mAbs, vol.7, pp.231-242, 2015.

K. Xue, R. Sarkar, C. Motz, S. Asami, D. C. Camargo et al., Limits of Resolution and Sensitivity of Proton Detected MAS Solid-State NMR Experiments at 111 kHz in Deuterated and Protonated Proteins, Scientific Reports, vol.7, p.7444, 2017.

K. Yaginuma, Y. Shirakata, M. Kobayashi, and K. Koike, Hepatitis B virus (HBV) particles are produced in a cell culture system by transient expression of transfected HBV DNA, Proceedings of the National Academy of Sciences, vol.84, pp.2678-2682, 1987.

K. Yamasaki, C. C. Weihl, and R. P. Roos, Alternative Translation Initiation of Theiler's Murine Encephalomyelitis Virus, J. VIROL, vol.73, 1999.

S. Yamauchi, N. Fusada, H. Hayashi, T. Utsumi, N. Uozumi et al., The consensus motif for Nmyristoylation of plant proteins in a wheat germ cell-free translation system: Cell-free N-myristoylation of plant proteins, FEBS Journal, vol.277, pp.3596-3607, 2010.

H. Yan and W. Li, Sodium Taurocholate Cotransporting Polypeptide Acts as a Receptor for Hepatitis B and D Virus, 2015.

, Dig Dis, vol.33, pp.388-396

H. Yan, B. Peng, W. He, G. Zhong, Y. Qi et al., Molecular Determinants of Hepatitis B and D Virus Entry Restriction in Mouse Sodium Taurocholate Cotransporting Polypeptide, Journal of Virology, vol.87, pp.7977-7991, 2013.

H. Yan, B. Peng, Y. Liu, G. Xu, W. He et al., Viral Entry of Hepatitis B and D Viruses and Bile Salts Transportation Share Common Molecular Determinants on Sodium Taurocholate Cotransporting Polypeptide, Journal of Virology, vol.88, pp.3273-3284, 2014.

H. Yan, G. Zhong, G. Xu, W. He, Z. Jing et al., Sodium taurocholate cotransporting polypeptide is a functional receptor for human hepatitis B and D virus, vol.1, p.49, 2012.

C. H. Yang and M. Cho, Hepatitis B virus X gene differentially modulates cell cycle progression and apoptotic protein expression in hepatocyte versus hepatoma cell lines: HBV X gene differentially modulates cell cycle progression, Journal of Viral Hepatitis, vol.20, pp.50-58, 2013.

C. Yang, E. Huang, H. Li, P. Su, and C. Shih, Nuclear Export of Human Hepatitis B Virus Core Protein and Pregenomic RNA Depends on the Cellular NXF1-p15 Machinery, PLoS ONE, vol.9, 2014.

L. Yang, Y. Wang, H. Chen, L. Shi, X. Tong et al., Effect of a hepatitis B virus inhibitor, NZ-4, on capsid formation, Antiviral Research, vol.125, pp.25-33, 2016.

W. Yang, J. Guo, Z. Ying, S. Hua, W. Dong et al., Capsid Assembly and Involved Function Analysis of Twelve Core Protein Mutants of Duck Hepatitis B Virus, Journal of Virology, vol.68, 1994.

J. Yokoyama, T. Matsuda, S. Koshiba, N. Tochio, and T. Kigawa, A practical method for cell-free protein synthesis to avoid stable isotope scrambling and dilution, Analytical Biochemistry, vol.411, pp.223-229, 2011.

X. Yu, L. Jin, J. Jih, C. Shih, H. Zhou et al., 3.5Å cryoEM Structure of Hepatitis B Virus Core Assembled from Full-Length Core Protein, PLoS ONE, vol.8, p.69729, 2013.
URL : https://hal.archives-ouvertes.fr/inria-00587377

Y. Yu, P. Wan, Y. Cao, W. Zhang, J. Chen et al., Hepatitis B Virus e Antigen Activates the Suppressor of Cytokine Signaling 2 to, Repress Interferon Action. Sci Rep, vol.7, p.1729, 2017.

M. Yuen, D. Chen, G. M. Dusheiko, H. L. Janssen, D. T. Lau et al., Hepatitis B virus infection, Nat Rev Dis Primers, vol.4, p.18035, 2018.
URL : https://hal.archives-ouvertes.fr/hal-01796201

A. Zajakina, T. Kozlovska, R. Bruvere, J. Aleksejeva, P. Pumpens et al., Translation of hepatitis B virus (HBV) surface proteins from the HBV pregenome and precore RNAs in Semliki Forest virus-driven expression, J. Gen. Virol, vol.85, pp.3343-3351, 2004.

P. C. Zamecnik and I. D. Frantz, Incorporation in vitro of radioactive carbon from carboxyl-labeled dl-alanine and glycine into proteins of normal and malignant rat livers, J Biol Chem, vol.175, pp.299-314, 1948.

R. Zampino, A. Boemio, C. Sagnelli, L. Alessio, L. E. Aldinolfi et al., Hepatitis B virus burden in developing countries, WJG, vol.21, p.11941, 2015.

T. Zapf, C. D. Tan, T. Reinelt, C. Huber, D. Shaohua et al., Synthesis and Functional Reconstitution of Light-Harvesting Complex II into Polymeric Membrane Architectures, Angewandte Chemie International Edition, vol.54, pp.14664-14668, 2015.

H. Zhang, G. G. Chen, B. Hu, Z. Zhang, J. Yun et al., Hepatitis B virus x protein induces autophagy via activating death-associated protein kinase, J Viral Hepat, vol.21, pp.642-649, 2014.

P. Zhang, S. Zhai, J. Chang, and J. Guo, In Vitro Anti-hepatitis B Virus Activity of 2?,3?-Dideoxyguanosine, Virol. Sin, vol.33, pp.538-544, 2018.

Y. Zhang, B. Zhang, D. Theele, S. Litwin, E. Toll et al., Single-cell analysis of covalently closed circular DNA copy numbers in a hepadnavirus-infected liver, Proceedings of the National Academy of Sciences, vol.100, pp.12372-12377, 2003.

Q. Zhao, V. Towne, M. Brown, Y. Wang, D. Abraham et al., In-depth process understanding of RECOMBIVAX HB® maturation and potential epitope improvements with redox treatment: Multifaceted biochemical and immunochemical characterization, Vaccine, vol.29, pp.7936-7941, 2011.

Q. Zheng, L. Bai, S. Zheng, M. Liu, J. Zhang et al., Efficient inhibition of duck hepatitis B virus DNA by the CRISPR/Cas9 system, Molecular Medicine Reports, vol.16, pp.7199-7204, 2017.

H. Zhou, J. Yong, H. Gao, T. Li, H. Xiao et al., Mannanase Man23 mutant library construction based on a novel cell-free protein expression system: Mannanase engineering and its expression, J. Sci. Food Agric, vol.97, pp.2199-2204, 2017.

A. Zlotnick, N. Cheng, J. F. Conway, F. P. Booy, A. C. Steven et al., Dimorphism of Hepatitis B Virus Capsids Is Strongly Influenced by the C-Terminus of the Capsid Protein, Biochemistry, vol.35, pp.7412-7421, 1996.

A. Zlotnick, N. Cheng, S. J. Stahl, J. F. Conway, A. C. Steven et al., Localization of the C terminus of the assembly domain of hepatitis B virus capsid protein: Implications for morphogenesis and organization of encapsidated RNA, Proceedings of the National Academy of Sciences, vol.94, pp.9556-9561, 1997.

A. Zlotnick, B. Venkatakrishnan, Z. Tan, E. Lewellyn, W. Turner et al., Core protein: A pleiotropic keystone in the HBV lifecycle, Antiviral Research, vol.121, pp.82-93, 2015.

W. L. Zoll, L. E. Horton, A. A. Komar, J. O. Hensold, and W. C. Merrick, Characterization of Mammalian eIF2A and Identification of the Yeast Homolog, J. Biol. Chem, vol.277, pp.37079-37087, 2002.

F. Zoulim, New insight on hepatitis B virus persistence from the study of intrahepatic viral cccDNA, Journal of Hepatology, vol.42, pp.302-308, 2005.

F. Zoulim and C. Seeger, Reverse Transcription in Hepatitis B Viruses Is Primed by a Tyrosine Residue of the Polymerase, vol.68, 1994.

G. Zubay, In vitro synthesis of protein in microbial systems, Annu Rev Genet, vol.7, pp.267-287, 1973.

E. R. Zuiderweg, Mapping Protein?Protein Interactions in Solution by, NMR Spectroscopy ? . Biochemistry, vol.41, pp.1-7, 2002.

L. B. Andreas, K. Jaudzems, J. Stanek, D. Lalli, A. Bertarello et al., Structure of fully protonated proteins by proton-detected magic-angle spinning NMR, Proc. Natl. Acad. Sci, vol.113, pp.9187-9192, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01359815

E. Barbet-massin, A. J. Pell, J. S. Retel, L. B. Andreas, K. Jaudzems et al., Rapid Proton-Detected NMR Assignment for Proteins with Fast Magic Angle Spinning, J. Am. Chem. Soc, vol.136, pp.12489-12497, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01070782

A. Böckmann, C. Gardiennet, R. Verel, A. Hunkeler, A. Loquet et al., Characterization of different water pools in solid-state NMR protein samples, J. Biomol. NMR, vol.45, pp.319-327, 2009.

G. R. Dreesman, F. B. Hollinger, and J. L. Melnick, Detection of Hepatitis B Antigen by Counter-Immunoelectrophoresis: Enhancing Role of Homologous Serum Diluents, Appl. Microbiol, vol.24, pp.1001-1002, 1972.

B. E. Eble, V. R. Lingappa, and D. Ganem, Hepatitis B surface antigen: an unusual secreted protein initially synthesized as a transmembrane polypeptide, Mol. Cell. Biol, vol.6, pp.1454-1463, 1986.

M. Fogeron, A. Badillo, V. Jirasko, J. Gouttenoire, D. Paul et al., Wheat germ cell-free expression: Two detergents with a low critical micelle concentration allow for production of soluble HCV membrane proteins, Protein Expr. Purif, vol.105, pp.39-46, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01075448

M. Fogeron, A. Badillo, F. Penin, and A. Bockmann, Wheat Germ Cell-Free Overexpression for the Production of Membrane Proteins, Methods Mol. Biol. Clifton NJ, vol.1635, pp.91-108, 2017.

M. Fogeron, V. Jirasko, S. Penzel, D. Paul, R. Montserret et al., Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus, J. Biomol. NMR, vol.65, pp.87-98, 2016.

M. Fogeron, D. Paul, V. Jirasko, R. Montserret, D. Lacabanne et al., Functional expression, purification, characterization, and membrane reconstitution of non-structural protein 2 from hepatitis C virus, Protein Expr. Purif, vol.116, pp.1-6, 2015.

F. Gavilanes, J. Gomez-gutierrez, M. Aracil, J. M. Gonzalez-ros, J. A. Ferragut et al., Hepatitis B surface antigen. Role of lipids in maintaining the structural and antigenic properties of protein components, Biochem. J, vol.265, pp.857-864, 1990.

V. J. Greiner, C. Egelé, S. Oncul, F. Ronzon, C. Manin et al., Characterization of the lipid and protein organization in HBsAg viral particles by steady-state and time-resolved fluorescence spectroscopy, Biochimie, vol.92, pp.994-1002, 2010.
URL : https://hal.archives-ouvertes.fr/hal-00508184

C. Guo, G. Hou, X. Lu, B. O'hare, J. Struppe et al., Fast magic angle spinning NMR with heteronucleus detection for resonance assignments and structural characterization of fully protonated proteins, J. Biomol. NMR, vol.60, pp.219-229, 2014.

F. Hagn, M. Etzkorn, T. Raschle, and G. Wagner, Optimized Phospholipid Bilayer Nanodiscs Facilitate High-Resolution Structure Determination of Membrane Proteins, J. Am. Chem. Soc, vol.135, pp.1919-1925, 2013.

E. Hardy, E. Mart??ez, D. Diago, R. D?áz, D. González et al., Large-scale production of recombinant hepatitis B surface antigen from Pichia pastoris, J. Biotechnol, vol.77, pp.157-167, 2000.

Y. Ishii, A. Wickramasinghe, I. Matsuda, Y. Endo, Y. Ishii et al., Progress in proton-detected solidstate NMR (SSNMR): Super-fast 2D SSNMR collection for nano-mole-scale proteins, J. Magn. Reson, vol.286, pp.99-109, 2018.

H. Kaur, A. Lakatos-karoly, R. Vogel, A. Nöll, R. Tampé et al., Coupled ATPase-adenylate kinase activity in ABC transporters, Nat. Commun, vol.7, p.13864, 2016.

C. Klammt, I. Maslennikov, M. Bayrhuber, C. Eichmann, N. Vajpai et al., Facile backbone structure determination of human membrane proteins by NMR spectroscopy, Nat. Methods, vol.9, pp.834-839, 2012.

A. Laguerre, F. Löhr, F. Bernhard, and V. Dötsch, Labeling of Membrane Proteins by Cell-Free Expression, Methods in Enzymology, pp.367-388, 2015.

D. Lalli, M. N. Idso, L. B. Andreas, S. Hussain, N. Baxter et al., Proton-Based Structural Analysis of a Heptahelical Transmembrane Protein in Lipid Bilayers, J. Am. Chem. Soc, vol.139, pp.13006-13012, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01587044

R. Linser, Solid-state NMR spectroscopic trends for supramolecular assemblies and protein aggregates, Solid State Nucl. Magn. Reson, vol.87, pp.45-53, 2017.

A. Mainz, T. L. Religa, R. Sprangers, R. Linser, L. E. Kay et al., NMR Spectroscopy of Soluble Protein Complexes at One Mega-Dalton and Beyond, Angew. Chem. Int. Ed, vol.52, pp.8746-8751, 2013.

S. Makino, E. T. Beebe, J. L. Markley, and B. G. Fox, Cell-Free Protein Synthesis for Functional and Structural Studies, Structural Genomics, pp.161-178, 2014.

W. S. Mason, G. Seal, and J. Summers, Virus of Pekin Ducks with Structural and Biological Relatedness to Human Hepatitis B Virus, J. Virol, vol.36, pp.829-836, 1980.

S. Penzel, A. A. Smith, V. Agarwal, A. Hunkeler, M. Org et al., Protein resonance assignment at MAS frequencies approaching 100 kHz: a quantitative comparison of J-coupling and dipolar-coupling-based transfer methods, 2015.

, Biomol. NMR, vol.63, pp.165-186

J. C. Pugh, Q. Di, W. S. Mason, and H. Simmons, Susceptibility to Duck Hepatitis B Virus Infection Is Associated with the Presence of Cell Surface Receptor Sites That Efficiently Bind Viral Particles, J. Virol, vol.69, p.9, 1995.

S. Reckel, D. Gottstein, J. Stehle, F. Löhr, M. Verhoefen et al., Solution NMR Structure of Proteorhodopsin, Angew. Chem. Int. Ed, vol.50, pp.11942-11946, 2011.

U. Schultz, E. Grgacic, and M. Nassal, Duck Hepatitis B Virus: An Invaluable Model System for HBV Infection, Advances in Virus Research, pp.63001-63007, 2004.

C. Seeger, F. Zoulim, and W. S. Mason, Hepadnavirus," in Fields Virology, pp.2185-2221, 2013.

S. Seitz, S. Urban, C. Antoni, and B. Böttcher, Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions, EMBO J, vol.26, pp.4160-4167, 2007.

J. Stanek, L. B. Andreas, K. Jaudzems, D. Cala, D. Lalli et al., NMR Spectroscopic Assignment of Backbone and Side-Chain Protons in Fully Protonated Proteins: Microcrystals, Sedimented Assemblies, and Amyloid Fibrils, 2016.

, Angew. Chem. Int. Ed, vol.55, pp.15504-15509

T. J. Stevens, R. H. Fogh, W. Boucher, V. A. Higman, F. Eisenmenger et al., A software framework for analysing solid-state MAS NMR data, J. Biomol. NMR, vol.51, pp.437-447, 2011.

H. J. Stirk, J. M. Thornton, and C. R. Howard, A topological model for hepatitis B surface antigen, Intervirology, vol.33, pp.148-158, 1992.

J. Struppe, C. M. Quinn, M. Lu, M. Wang, G. Hou et al., Expanding the horizons for structural analysis of fully protonated protein assemblies by NMR spectroscopy at MAS frequencies above 100 kHz, Solid State Nucl. Magn. Reson, vol.87, pp.117-125, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01575525

T. Sugiki, O. Ichikawa, M. Miyazawa-onami, I. Shimada, and H. Takahashi, Isotopic Labeling of Heterologous Proteins in the Yeast Pichia pastoris and Kluyveromyces lactis, Protein NMR Techniques, pp.19-36, 2012.

K. Takai, T. Sawasaki, and Y. Endo, Practical cell-free protein synthesis system using purified wheat embryos, Nat. Protoc, vol.5, pp.227-238, 2010.

M. Takeda and M. Kainosho, Cell-Free Protein Synthesis Using E. coli Cell Extract for NMR Studies, Advances in Experimental Medicine and Biology, pp.167-177, 2012.

T. Terada, Y. , and S. , Escherichia coli Cell-Free Protein Synthesis and Isotope Labeling of Mammalian Proteins, Methods in Enzymology, pp.311-345, 2015.

P. Valenzuela, A. Medina, W. J. Rutter, G. Ammerer, and B. D. Hall, Synthesis and assembly of hepatitis B virus surface antigen particles in yeast, Nature, vol.298, pp.347-350, 1982.

M. Wang, C. M. Quinn, J. R. Perilla, H. Zhang, R. Shirra et al., Quenching protein dynamics interferes with HIV capsid maturation, Nat. Commun, vol.8, p.1779, 2017.

S. Wang and V. Ladizhansky, Recent advances in magic angle spinning solid state NMR of membrane proteins, Prog. Nucl. Magn. Reson. Spectrosc, vol.82, pp.1-26, 2014.

S. Wang, S. Parthasarathy, Y. Xiao, Y. Nishiyama, F. Long et al., Nano-mole Scale Sequential Signal Assignment by 1H-Detected Protein Solid-state NMR using Ultra-Fast Magic-Angle Spinning and HIGHLIGHT Spectral Editing, Chem. Commun, vol.51, pp.15055-15058, 2015.

M. Zahid, H. Lünsdorf, and U. Rinas, Assessing stability and assembly of the hepatitis B surface antigen into viruslike particles during down-stream processing, Vaccine, vol.33, pp.3739-3745, 2015.

R. Zhang, K. H. Mroue, and A. Ramamoorthy, Proton-Based Ultrafast Magic Angle Spinning Solid-State NMR Spectroscopy, Acc. Chem. Res, vol.50, pp.1105-1113, 2017.

A. Abdine, M. A. Verhoeven, and D. E. Warschawski, Cell-free expression and labeling strategies for a new decade in solid-state NMR, New Biotechnol, vol.28, pp.272-276, 2011.
URL : https://hal.archives-ouvertes.fr/hal-02567621

T. Arakawa and S. N. Timasheff, Preferential interactions of proteins with salts in concentrated solutions, Biochemistry, vol.21, pp.6545-6552, 1982.

L. J. Braun, J. Jezek, S. Peterson, A. Tyagi, S. Perkins et al., Characterization of a thermostable hepatitis B vaccine formulation, Vaccine, vol.27, pp.4609-4614, 2009.

C. P. Connern, Chaotropic Agents and Increased Matrix Volume Enhance Binding of Mitochondrial Cyclophilin to the Inner Mitochondrial Membrane and Sensitize the Mitochondrial Permeability Transition to [Ca2+, Biochemistry, vol.35, pp.8172-8180, 1996.

D. F. Davidson and D. J. Watson, Macroenzyme detection by polyethylene glycol precipitation, Ann. Clin. Biochem, vol.40, pp.514-520, 2003.

D. Deville-bonne, G. L. Bras, W. Teschner, and J. R. Garel, Ordered disruption of subunit interfaces during the stepwise reversible dissociation of Escherichia coli phosphofructokinase with potassium thiocyanate, Biochemistry, vol.28, pp.1917-1922, 1989.

D. Diminsky, R. Schirmbeck, J. Reimann, and Y. Barenholz, Comparison between hepatitis B surface antigen (HBsAg) particles derived from mammalian cells (CHO) and yeast cells (Hansen&a polymorpha): composition, structure and immunogenicity, Vaccine, vol.15, pp.637-647, 1997.

K. C. Duong-ly and S. B. Gabelli, Salting out of Proteins Using Ammonium Sulfate Precipitation, Methods in Enzymology, pp.85-94, 2014.

M. Einarsson, L. Kaplan, and G. Utter, Purification of Hepatitis B Surface Antigen by Affinity Chromatography, Vox Sang, vol.35, pp.224-233, 1978.

W. M. Fogarty and P. J. Griffin, Production and Purification of the Metalloprotease of Bacillus polymyxa, Appl. Microbiol, vol.26, p.6, 1973.

M. Fogeron, D. Paul, V. Jirasko, R. Montserret, D. Lacabanne et al., Functional expression, purification, characterization, and membrane reconstitution of non-structural protein 2 from hepatitis C virus, Protein Expr. Purif, vol.116, pp.1-6, 2015.

H. Fraga, C. Arnaud, D. F. Gauto, M. Audin, V. Kurauskas et al., Solid-State NMR H-N-(C)-H and H-N-C-C 3D/4D Correlation Experiments for Resonance Assignment of Large Proteins, ChemPhysChem, vol.18, pp.2697-2703, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01583214

A. C. French, A. L. Thompson, and B. G. Davis, High-purity discrete PEG-oligomer crystals allow structural insight, 2009.

, Angew. Chem. Int. Ed Engl, vol.48, pp.1248-1252

E. Gerhardt and V. Bruss, Phenotypic Mixing of Rodent but Not Avian Hepadnavirus Surface Proteins into Human Hepatitis B Virus Particles, J. Virol, vol.69, 1995.

R. B. Gibson and E. J. Banzhaf, The Quantitative Changes in the Proteins in the Blood Plasma of Horses in the Course of Immunization, J. Exp. Med, vol.12, pp.411-434, 1910.

R. J. Gilbert, L. Beales, D. Blond, M. N. Simon, B. Y. Lin et al., Hepatitis B small surface antigen particles are octahedral, Proc. Natl. Acad. Sci, vol.102, pp.14783-14788, 2005.

J. P. Goldring, Methods to Concentrate Proteins for Protein Isolation, Proteomic, and Peptidomic Evaluation, Methods in Molecular Biology, pp.5-18, 2015.

J. P. Goldring, Three-Phase Partitioning, Dialysis, Centrifugation, Ultrafiltration, Lyophilization, Affinity Chromatography, Immunoprecipitation or Increased Temperature for Protein Isolation, Drug Interaction, and Proteomic and Peptidomic Evaluation, Electrophoretic Separation of Proteins, pp.41-59, 2019.

P. Guo, Y. El-gohary, K. Prasadan, C. Shiota, X. Xiao et al., Rapid and simplified purification of recombinant adeno-associated virus, J. Virol. Methods, vol.183, pp.139-146, 2012.

C. Gurramkonda, M. Zahid, S. K. Nemani, A. Adnan, S. K. Gudi et al., Purification of hepatitis B surface antigen virus-like particles from recombinant Pichia pastoris and in vivo analysis of their immunogenic properties, J. Chromatogr. B Analyt. Technol. Biomed. Life. Sci, vol.940, pp.104-111, 2013.

B. Hoffmann, F. Löhr, A. Laguerre, F. Bernhard, and V. Dötsch, Protein labeling strategies for liquid-state NMR spectroscopy using cell-free synthesis, Prog. Nucl. Magn. Reson. Spectrosc, vol.105, pp.1-22, 2018.

K. C. Ingham, Precipitation of proteins with polyethylene glycol, Methods Enzymol, vol.182, pp.301-306, 1990.

R. F. Itzhaki, Structure and Properties of Rat Thymus Deoxyribonucleoprotein, Biochem. J, vol.105, pp.741-748, 1967.

J. Jezek, D. Chen, L. Watson, J. Crawford, S. Perkins et al., A heat-stable hepatitis B vaccine formulation, Hum. Vaccin, vol.5, pp.529-535, 2009.

M. Kainosho and T. Tsuji, Assignment of the three methionyl carbonyl carbon resonances in Streptomyces subtilisin inhibitor by a carbon-13 and nitrogen-15 double-labeling technique. A new strategy for structural studies of proteins in solution, Biochemistry, vol.21, pp.6273-6279, 1982.

T. Kigawa, Y. Muto, Y. , and S. , Cell-free synthesis and amino acid-selective stable isotope labeling of proteins for NMR analysis, J. Biomol. NMR, vol.6, 1995.

K. Y. Ko and D. U. Ahn, Preparation of immunoglobulin Y from egg yolk using ammonium sulfate precipitation and ion exchange chromatography, Poult. Sci, vol.86, pp.400-407, 2007.

B. Kunert, C. Gardiennet, D. Lacabanne, D. Calles-garcia, P. Falson et al., Efficient and stable reconstitution of the ABC transporter BmrA for solid-state NMR studies, Front. Mol. Biosci, vol.1, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01140511

R. H. Kutner, X. Zhang, and J. Reiser, Production, concentration and titration of pseudotyped HIV-1-based lentiviral vectors, Nat. Protoc, vol.4, pp.495-505, 2009.

D. Lacabanne, A. Lends, C. Danis, B. Kunert, M. Fogeron et al., Gradient reconstitution of membrane proteins for solid-state NMR studies, J. Biomol. NMR, vol.69, pp.81-91, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02329453

D. Lacabanne, B. H. Meier, and A. Böckmann, Selective labeling and unlabeling strategies in protein solid-state NMR spectroscopy, J. Biomol. NMR, vol.71, pp.141-150, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02322201

G. D. Lewis and T. G. Metcalf, Polyethylene Glycol Precipitation for Recovery of Pathogenic Viruses, Including Hepatitis A Virus and Human Rotavirus, from Oyster, Water, and Sediment Samples, Appl. Environ. Microbiol, vol.54, 1983.

J. L. Lopes, D. C. Oliveira, C. L. Utescher, W. Quintilio, E. C. Tenório et al., Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions, Vaccine, vol.37, pp.6415-6425, 2019.

H. Lünsdorf, C. Gurramkonda, A. Adnan, N. Khanna, and U. Rinas, Virus-like particle production with yeast: ultrastructural and immunocytochemical insights into Pichia pastoris producing high levels of the Hepatitis B surface antigen. Microb, Cell Factories, vol.10, p.48, 2011.

C. M. Mangold and R. E. Streeck, Mutational Analysis of the Cysteine Residues in the Hepatitis B Virus Small Envelope Protein, J. Virol, vol.67, p.10, 1993.

A. Mcpherson, Protein Crystallization, Protein Crystallography, pp.17-50, 2017.

A. Moreno, Advanced Methods of Protein Crystallization, Methods Mol. Biol, pp.51-76, 2017.

A. R. Neurath, A. M. Prince, and J. Giacalone, Large-scale purification of hepatitis B surface antigen using affinity chromatography, Experientia, vol.34, pp.414-415, 1978.

A. Polson, Purification and aggregation of influenza virus by precipitation with polyethylene glycol, Prep. Biochem, vol.23, pp.207-225, 1974.

A. Polson, G. M. Potgieter, J. F. Largier, and G. E. Mears, The Fractionation of Protein Mixtures by Linear Polymers of High Molecular Weight, Biochim Biophys Acta, vol.82, p.13, 1964.

O. Satoh, H. Imai, T. Yoneyama, T. Miyamura, H. Utsumi et al., Membrane structure of the hepatitis B virus surface antigen particle, J. Biochem. (Tokyo), vol.127, pp.543-550, 2000.

T. G. Schmidt and A. Skerra, The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins, Nat. Protoc, vol.2, pp.1528-1535, 2007.

R. K. Scopes, Strategies for Protein Purification, Current Protocols in Protein Science, 1995.

D. W. Dunn, P. T. Speicher, and . Wingfield,

S. Sim, T. He, A. Tscheliessnig, M. Mueller, R. B. Tan et al., Branched polyethylene glycol for protein precipitation, Biotechnol. Bioeng, vol.109, pp.736-746, 2012.

X. Su, C. Loh, R. Qi, and G. Otting, Suppression of isotope scrambling in cell-free protein synthesis by broadband inhibition of PLP enymes for selective 15N-labelling and production of perdeuterated proteins in H2O, J. Biomol. NMR, vol.50, pp.35-42, 2011.

D. A. Torchia, S. W. Sparks, and A. Bax, Staphylococcal nuclease: sequential assignments and solution structure, Biochemistry, vol.28, pp.5509-5524, 1989.

S. Wang, M. Fogeron, M. Schledorn, M. Dujardin, S. Penzel et al., Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation, Front. Mol. Biosci, vol.6, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02322693

P. S. Wu, K. Ozawa, S. Jergic, X. Su, N. E. Dixon et al., Amino-acid Type Identification in 15N-HSQC Spectra by Combinatorial Selective 15N-labelling, J. Biomol. NMR, vol.34, pp.13-21, 2006.

M. Zahid, H. Lünsdorf, and U. Rinas, Assessing stability and assembly of the hepatitis B surface antigen into viruslike particles during down-stream processing, Vaccine, vol.33, pp.3739-3745, 2015.

A. , Topology model of the DHBs L protein in "internal" (or i-DpreS) conformation upon translation, then "external, 1992.

B. Grgacic, Alternative translation initiation is observed on DHBs L WG-CFPS We have recently reported WG-CFPS of DHBs S, which autoassembles during expression in structures called subviral particles (SVPs, bilayer method, 1998.

C. , Two constructs of DHBs L were used, carrying either a StrepTag II, 2007.

F. ;. Sud and . Fogeron, , 2010.

. Fogeron, 1U/?l RNase inhibitor (CellFreeSciences, Japan) and 1U/?l SP6 RNA polymerase (CellFreeSciences, 2010.

. Fogeron, DDM, as described previously, 2015.

, -gel digestion for mass spectrometry

(. Amanda and . Dorfer, , 2014.

, Da, and up to 2 missed cleavages were allowed

, Oxidation (M), acetylation (Protein N-terminus) and Phosphorylation (S, T, Y) were set as variable modification, and Carbamidomethylation (C)

A. Badillo, V. Receveur-brechot, S. Sarrazin, F. Cantrelle, F. Delolme et al., Overall Structural Model of NS5A Protein from Hepatitis C Virus and Modulation by Mutations Confering Resistance of Virus Replication to Cyclosporin A, Biochemistry, vol.56, pp.3029-3048, 2017.
URL : https://hal.archives-ouvertes.fr/hal-01785410

G. A. Bazykin and A. V. Kochetov, Alternative translation start sites are conserved in eukaryotic genomes, Nucleic Acids Res, vol.39, pp.567-577, 2011.

V. Bruss and R. Thomssen, , 1994.

P. S. Chae, S. G. Rasmussen, R. R. Rana, K. Gotfryd, R. Chandra et al., Maltose-neopentyl glycol (MNG) amphiphiles for solubilization, stabilization and crystallization of membrane proteins, Nat. Methods, vol.7, pp.1003-1008, 2010.

A. Chen, N. Panjaworayan-t-thienprasert, and C. M. Brown, Prospects for inhibiting the post-transcriptional regulation of gene expression in hepatitis B virus, World J. Gastroenterol, vol.20, p.7993, 2014.

S. Chi, D. Kim, S. Lee, I. Chang, and K. Han, Pre-structured motifs in the natively unstructured preS1 surface antigen of hepatitis B virus, Protein Sci, vol.16, pp.2108-2117, 2007.

G. David, M. Fogeron, M. Schledorn, R. Montserret, U. Haselmann et al., Structural Studies of Self-Assembled Subviral Particles: Combining Cell-Free Expression with 110 kHz MAS NMR Spectroscopy, Angew. Chem. Int. Ed, vol.57, pp.4787-4791, 2018.
URL : https://hal.archives-ouvertes.fr/hal-02322342

R. J. Davis, The mitogen-activated protein kinase signal transduction pathway, J. Biol. Chem, vol.268, pp.14553-14556, 1993.

R. B. Denman, Protein Methyltransferase Activities in Commercial In vitro Translation Systems, J. Biochem. (Tokyo), vol.144, pp.223-233, 2008.

V. Dorfer, P. Pichler, T. Stranzl, J. Stadlmann, T. Taus et al., MS Amanda, a Universal Identification Algorithm Optimized for High Accuracy Tandem Mass Spectra, J. Proteome Res, vol.13, pp.3679-3684, 2014.

J. K. Eng, A. L. Mccormack, and J. R. Yates, , 1994.

, J. Am. Soc. Mass Spectrom, vol.5, pp.976-989

D. Fernholz, G. Wildner, W. , and H. , Minor envelope proteins of duck hepatitis B virus are initiated at internal pre-S AUG codons but are not essential for infectivity, Virology, vol.197, pp.64-73, 1993.

M. Fogeron, A. Badillo, V. Jirasko, J. Gouttenoire, D. Paul et al., Wheat germ cell-free expression: Two detergents with a low critical micelle concentration allow for production of soluble HCV membrane proteins, Protein Expr. Purif, vol.105, pp.39-46, 2015.
URL : https://hal.archives-ouvertes.fr/hal-01075448

M. Fogeron, A. Badillo, F. Penin, and A. Böckmann, Wheat Germ Cell-Free Overexpression for the Production of Membrane Proteins, Membrane Protein Structure and Function Characterization, pp.91-108, 2017.

M. Fogeron, V. Jirasko, S. Penzel, D. Paul, R. Montserret et al., Cell-free expression, purification, and membrane reconstitution for NMR studies of the nonstructural protein 4B from hepatitis C virus, J. Biomol. NMR, vol.65, pp.87-98, 2016.

M. Fogeron, D. Paul, V. Jirasko, R. Montserret, D. Lacabanne et al., Functional expression, purification, characterization, and membrane reconstitution of non-structural protein 2 from hepatitis C virus, Protein Expr. Purif, vol.116, pp.1-6, 2015.

N. Fouillot, S. Tlouzeau, J. Rossignol, J. , and O. , Translation of the Hepatitis B Virus P Gene by Ribosomal Scanning as an Alternative to Internal Initiation, J. Gen. Virol, vol.67, p.10, 1993.

J. Fütterer, Z. Kiss-lászló, and T. Hohn, Nonlinear ribosome migration on cauliflower mosaic virus 35S RNA, Cell, vol.73, issue.93, p.90257, 1993.

E. V. Grgacic, D. A. Anderson, B. Lin, M. J. Snooks, and E. V. Gazina, Normal phosphorylation of duck hepatitis B virus L protein is dispensable for infectivity, J. Gen. Virol, vol.79, pp.2743-2751, 1998.

E. V. Grgacic, A. , and D. A. , The Large Surface Protein of Duck Hepatitis B Virus Is Phosphorylated in the Pre-S Domain, J. Virol, vol.68, p.7, 1994.

M. Harbers, Wheat germ systems for cell-free protein expression, FEBS Lett, vol.588, pp.2762-2773, 2014.

R. O. Heuckeroth, D. A. Towler, S. P. Adams, L. Glaser, G. et al., 11-(Ethylthio)undecanoic acid. A myristic acid analogue of altered hydrophobicity which is functional for peptide N-myristoylation with wheat germ and yeast acyltransferase, J. Biol. Chem, vol.263, pp.2127-2133, 1988.

B. D. Hopkins, B. Fine, N. Steinbach, M. Dendy, Z. Rapp et al., A Secreted PTEN Phosphatase That Enters Cells to Alter Signaling and Survival, Science, vol.341, pp.399-402, 2013.

R. C. Jackson and G. Blobel, Post-translational cleavage of presecretory proteins with an extract of rough microsomes from dog pancreas containing signal peptidase activity, Proc. Natl. Acad. Sci, vol.74, pp.5598-5602, 1977.

M. C. Jürgens, J. Vörös, G. J. Rautureau, D. A. Shepherd, V. E. Pye et al., The hepatitis B virus preS1 domain hijacks host trafficking proteins by motif mimicry, Nat. Chem. Biol, vol.9, pp.540-547, 2013.

U. Klingmüller and H. Schaller, Hepadnavirus Infection Requires Interaction between the Viral Pre-S Domain and a Specific Hepatocellular Receptor, J. Virol, vol.67, pp.7414-7422, 1993.

A. V. Kochetov, A. Sarai, I. B. Rogozin, V. K. Shumny, and N. A. Kolchanov, The role of alternative translation start sites in the generation of human protein diversity, Mol. Genet. Genomics, vol.273, pp.491-496, 2005.

H. Liang, W. Hittelman, and L. Nagarajan, Ubiquitous Expression and Cell Cycle Regulation of the Protein Kinase PIM-1, Arch. Biochem. Biophys, vol.330, pp.259-265, 1996.

D. R. Macrae, V. Bruss, and D. Ganem, Myristylation of a duck hepatitis B virus envelope protein is essential for infectivity but not for virus assembly, Virology, vol.181, pp.359-363, 1991.

K. Matsumoto, C. Tomikawa, T. Toyooka, A. Ochi, Y. Takano et al., Production of yeast tRNA (m7G46) methyltransferase (Trm8-Trm82 complex) in a wheat germ cell-free translation system, J. Biotechnol, vol.133, pp.453-460, 2008.

Y. Mak, D. J. Skylas, R. Willows, A. Connolly, S. J. Cordwell et al., A proteomic approach to the identification and characterisation of protein composition in wheat germ, Funct. Integr. Genomics, vol.6, pp.322-337, 2006.

F. Noordeen, C. A. Scougall, A. Grosse, Q. Qiao, B. B. Ajilian et al., Therapeutic Antiviral Effect of the Nucleic Acid Polymer REP 2055 against Persistent Duck Hepatitis B Virus Infection, PLoS ONE, vol.10, 2015.

K. Rothmann, M. S. Lzer, G. Radziwill, E. Hildt, K. Moelling et al., Host Cell-Virus Cross Talk: Phosphorylation of a Hepatitis B Virus Envelope Protein Mediates Intracellular Signaling, J. Virol, vol.72, p.10, 1998.

H. J. Schlicht, C. Kuhn, B. Guhr, &. Schaller, H. Mattaliano et al., Biochemical and Immunological Characterization of the Duck Hepatitis B Virus Envelope Proteins, J. Virol, vol.61, pp.2280-2885, 1987.

T. G. Schmidt and A. Skerra, The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins, Nat. Protoc, vol.2, pp.1528-1535, 2007.

U. Schultz, E. Grgacic, and M. Nassal, Duck Hepatitis B Virus: An Invaluable Model System for HBV Infection, Advances in Virus Research, pp.63001-63007, 2004.

R. Schweet, H. Lamfrom, A. , and E. , The Synthesis of Hemoglobin in a Cell-Free System, Biochemistry, vol.44, p.7, 1958.

N. Sen, F. Cao, and J. E. Tavis, Translation of Duck Hepatitis B Virus Reverse Transcriptase by Ribosomal Shunting, 2004.

. Virol, , vol.78, pp.11751-11757

G. E. Smith, M. D. Summers, and M. J. Fraser, Production of human beta interferon in insect cells infected with a baculovirus expression vector, Mol. Cell. Biol, vol.3, pp.2156-2165, 1983.

H. J. Stirk, J. M. Thornton, and C. R. Howard, A topological model for hepatitis B surface antigen, Intervirology, vol.33, pp.148-158, 1992.

I. Swameye and H. Schaller, Dual Topology of the Large Envelope Protein of Duck Hepatitis B Virus: Determinants Preventing Pre-S Translocation and Glycosylation, J. Virol, vol.71, 1997.

K. Takai, T. Sawasaki, and Y. Endo, Practical cell-free protein synthesis system using purified wheat embryos, Nat. Protoc, vol.5, pp.227-238, 2010.

J. A. Ubersax, E. L. Woodbury, P. N. Quang, M. Paraz, J. D. Blethrow et al., Targets of the cyclindependent kinase Cdk1, Nature, vol.425, pp.859-864, 2003.

L. A. Weber, E. R. Feman, and C. Baglioni, A Cell Free System from HeLa Cells Active in Initiation of Protein Synthesis, Biochemistry, vol.14, pp.5315-5321, 1975.

A. Zajakina, T. Kozlovska, R. Bruvere, J. Aleksejeva, P. Pumpens et al., Translation of hepatitis B virus (HBV) surface proteins from the HBV pregenome and precore RNAs in Semliki Forest virus-driven expression, J. Gen. Virol, vol.85, pp.3343-3351, 2004.

A. Zemella, L. Thoring, C. Hoffmeister, and S. Kubick, Cell-Free Protein Synthesis: Pros and Cons of Prokaryotic and Eukaryotic Systems, ChemBioChem, vol.16, pp.2420-2431, 2015.

Q. Zheng, L. Bai, S. Zheng, M. Liu, J. Zhang et al., Efficient inhibition of duck hepatitis B virus DNA by the CRISPR/Cas9 system, Mol. Med. Rep, vol.16, pp.7199-7204, 2017.

J. Guo and J. C. Pugh, Topology of the Large Envelope Protein of Duck Hepatitis B Virus Suggests a Mechanism for Membrane Translocation during Particle Morphogenesis, J. Virol, vol.71, 1997.

M. Nishi, A. Ryo, N. Tsurutani, K. Ohba, T. Sawasaki et al., Requirement for microtubule integrity in the SOCS1-mediated intracellular dynamics of HIV-1 Gag, FEBS Lett, vol.583, pp.1243-1250, 2009.

U. Schultz, E. Grgacic, and M. Nassal, Duck Hepatitis B Virus: An Invaluable Model System for HBV Infection, Advances in Virus Research, pp.63001-63007, 2004.

S. Wang, M. Fogeron, M. Schledorn, M. Dujardin, S. Penzel et al., Combining Cell-Free Protein Synthesis and NMR Into a Tool to Study Capsid Assembly Modulation, Front. Mol. Biosci, vol.6, 2019.
URL : https://hal.archives-ouvertes.fr/hal-02322693

E. V. Grgacic, D. A. Anderson, B. Lin, M. J. Snooks, and E. V. Gazina, Normal phosphorylation of duck hepatitis B virus L protein is dispensable for infectivity, J. Gen. Virol, vol.79, pp.2743-2751, 1998.

J. L. Lopes, D. C. Oliveira, C. L. Utescher, W. Quintilio, E. C. Tenório et al., , 2019.

, Antigenic and physicochemical characterization of Hepatitis B surface protein under extreme temperature and pH conditions, Vaccine, vol.37, pp.6415-6425

T. G. Schmidt, L. Batz, L. Bonet, U. Carl, G. Holzapfel et al., Development of the Twin-Strep-tag and its application for purification of recombinant proteins from cell culture supernatants, 2013.