J. S. Cox, B. Chen, M. Mcneil, W. R. Jacobs, and J. , Complex lipid determines tissuespecific replication of Mycobacterium tuberculosis in mice, Nature, vol.402, pp.79-83, 1999.

J. Yu, Both phthiocerol dimycocerosates and phenolic glycolipids are required for virulence of Mycobacterium marinum, Infect Immun, vol.80, pp.1381-1389, 2012.

C. J. Cambier, Mycobacteria manipulate macrophage recruitment through coordinated use of membrane lipids, Nature, vol.505, pp.218-222, 2014.

P. Domenech, M. B. Reed, and C. E. Barry, Contribution of the Mycobacterium tuberculosis MmpL protein family to virulence and drug resistance, Infect Immun, vol.3, pp.3492-3501, 2005.

L. Alibaud, A Mycobacterium marinum TesA mutant defective for major cell wall-associated lipids is highly attenuated in Dictyostelium discoideum and zebrafish embryos, Mol Microbiol, vol.80, pp.919-934, 2011.
URL : https://hal.archives-ouvertes.fr/hal-00641589

J. T. Belisle, L. Pascopella, J. M. Inamine, P. J. Brennan, W. R. Jacobs et al., Isolation and expression of a gene cluster responsible for biosynthesis of the glycopeptidolipid antigens of Mycobacterium avium, J Bacteriol, vol.173, pp.6991-6997, 1991.

A. Pawlik, Identification and characterization of the genetic changes responsible for the characteristic smooth-to-rough morphotype alterations of clinically persistent Mycobacterium abscessus, Mol Microbiol, vol.90, pp.612-629, 2013.

B. Sondén, Gap, a mycobacterial specific integral membrane protein, is required for glycolipid transport to the cell surface, Mol Microbiol, vol.58, pp.426-440, 2005.

H. Billman-jacobe, Glycopeptidolipid synthesis in mycobacteria, Curr Sci, vol.86, pp.111-114, 2004.

T. F. Byrd and C. R. Lyons, Preliminary characterization of a Mycobacterium abscessus mutant in human and murine models of infection, Infect Immun, vol.67, pp.4700-4707, 1999.

E. Catherinot, Acute respiratory failure involving an R variant of Mycobacterium abscessus, J Clin Microbiol, vol.47, pp.271-274, 2009.

A. Bernut, Insights into the smooth-to-rough transitioning in Mycobacterium bolletii unravels a functional Tyr residue conserved in all mycobacterial MmpL family members, Mol Microbiol, vol.99, pp.866-883, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02137603

A. Bernut, J. Herrmann, D. Ordway, and L. Kremer, The diverse cellular and animal models to decipher the physiopathological traits of Mycobacterium abscessus infection, Front Cell Infect Microbiol, vol.7, p.100, 2017.

K. M. Kreutzfeldt, Molecular longitudinal tracking of Mycobacterium abscessus spp. during chronic infection of the human lung, PLoS One, vol.8, p.63237, 2013.

B. E. Jönsson, Molecular epidemiology of Mycobacterium abscessus, with focus on cystic fibrosis, J Clin Microbiol, vol.45, pp.1497-1504, 2007.

T. Qvist, Comparing the harmful effects of nontuberculous mycobacteria and Gram negative bacteria on lung function in patients with cystic fibrosis, J Cyst Fibros, vol.15, pp.380-385, 2016.

E. Catherinot, Hypervirulence of a rough variant of the Mycobacterium abscessus type strain, Infect Immun, vol.75, pp.1055-1058, 2007.

A. Bernut, Mycobacterium abscessus cording prevents phagocytosis and promotes abscess formation, Proc Natl Acad Sci, vol.111, pp.943-952, 2014.
URL : https://hal.archives-ouvertes.fr/hal-02088315

J. Whang, Mycobacterium abscessus glycopeptidolipids inhibit macrophage apoptosis and bacterial spreading by targeting mitochondrial cyclophilin D, Cell Death Dis, vol.8, p.3012, 2017.

R. Brosch, Comparative genomics of the mycobacteria, Int J Med Microbiol, vol.290, pp.143-152, 2000.

A. Viljoen, The diverse family of MmpL transporters in mycobacteria: From regulation to antimicrobial developments, Mol Microbiol, vol.104, pp.889-904, 2017.
URL : https://hal.archives-ouvertes.fr/hal-02137585

C. Chalut, MmpL transporter-mediated export of cell-wall associated lipids and siderophores in mycobacteria, Tuberculosis (Edinb), vol.100, pp.32-45, 2016.

C. Dupont, A new piperidinol derivative targeting mycolic acid transport in Mycobacterium abscessus, Mol Microbiol, vol.101, pp.515-529, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02137602

A. P. Kozikowski, Targeting mycolic acid transport by Indole-2-carboxamides for the treatment of Mycobacterium abscessus infections, J Med Chem, vol.60, pp.5876-5888, 2017.

A. Viljoen, Controlling extra-and intramacrophagic Mycobacterium abscessus by targeting mycolic acid transport, Front Cell Infect Microbiol, vol.7, p.388, 2017.

H. Medjahed and J. Reyrat, Construction of Mycobacterium abscessus defined glycopeptidolipid mutants: Comparison of genetic tools, Appl Environ Microbiol, vol.75, pp.1331-1338, 2009.

S. Burbaud, Trehalose polyphleates are produced by a glycolipid biosynthetic pathway conserved across phylogenetically distant mycobacteria, Cell Chem Biol, vol.23, pp.278-289, 2016.

M. Llorens-fons, Trehalose polyphleates, external cell wall lipids in Mycobacterium abscessus, are associated with the formation of clumps with cording morphology, which have been associated with virulence, Front Microbiol, vol.8, p.1402, 2017.

L. Laencina, Identification of genes required for Mycobacterium abscessus growth in vivo with a prominent role of the ESX-4 locus, Proc Natl Acad Sci, vol.115, pp.1002-1011, 2018.
URL : https://hal.archives-ouvertes.fr/pasteur-02046027

G. Etienne, Identification of the polyketide synthase involved in the biosynthesis of the surface-exposed lipooligosaccharides in mycobacteria, J Bacteriol, vol.191, pp.2613-2621, 2009.

P. E. Kolattukudy, N. D. Fernandes, A. K. Azad, A. M. Fitzmaurice, and T. D. Sirakova, Biochemistry and molecular genetics of cell-wall lipid biosynthesis in mycobacteria, Mol Microbiol, vol.24, pp.263-270, 1997.

N. Bakala and J. C. Goma, Mycobacterium abscessus phospholipase C expression is induced during coculture within amoebae and enhances M. abscessus virulence in mice, Infect Immun, vol.83, pp.780-791, 2015.

H. Medjahed and A. K. Singh, Genetic manipulation of Mycobacterium abscessus, Curr Protoc Microbiol Chapter, 2010.

K. Pethe, Isolation of Mycobacterium tuberculosis mutants defective in the arrest of phagosome maturation, Proc Natl Acad Sci, vol.101, pp.13642-13647, 2004.

C. J. Queval, R. Brosch, and R. Simeone, The macrophage: A disputed fortress in the battle against Mycobacterium tuberculosis, Front Microbiol, vol.8, p.2284, 2017.
URL : https://hal.archives-ouvertes.fr/pasteur-02046252

A. C. Collins, Cyclic GMP-AMP synthase is an innate immune DNA sensor for Mycobacterium tuberculosis, Cell Host Microbe, vol.17, pp.820-828, 2015.

A. Kupz, ESAT-6-dependent cytosolic pattern recognition drives noncognate tuberculosis control in vivo, J Clin Invest, vol.126, pp.2109-2122, 2016.

R. Wassermann, Mycobacterium tuberculosis differentially activates cGASand inflammasome-dependent intracellular immune responses through ESX-1, Cell Host Microbe, vol.17, pp.799-810, 2015.

R. O. Watson, The cytosolic sensor cGAS detects Mycobacterium tuberculosis DNA to induce type I interferons and activate autophagy, Cell Host Microbe, vol.17, pp.811-819, 2015.

A. Bernut, Deciphering and imaging pathogenesis and cording of Mycobacterium abscessus in zebrafish embryos, J Vis Exp, vol.103, p.53130, 2015.
URL : https://hal.archives-ouvertes.fr/hal-02086982

I. Halloum, Deletion of a dehydratase important for intracellular growth and cording renders rough Mycobacterium abscessus avirulent, Proc Natl Acad Sci, vol.113, pp.4228-4237, 2016.
URL : https://hal.archives-ouvertes.fr/hal-02086925

J. Indrigo, R. L. Hunter, . Jr, and J. K. Actor, Cord factor trehalose 6,6?-dimycolate (TDM) mediates trafficking events during mycobacterial infection of murine macrophages, Microbiology, vol.149, pp.2049-2059, 2003.

C. Andréjak, Chronic respiratory disease, inhaled corticosteroids and risk of non-tuberculous mycobacteriosis, Thorax, vol.68, pp.256-262, 2013.

H. Chu, Prevalence of nontuberculous mycobacteria in patients with bronchiectasis: A meta-analysis, Arch Med Sci, vol.10, pp.661-668, 2014.

K. N. Olivier, Nontuberculous Mycobacteria in Cystic Fibrosis Study Group (2003) Nontuberculous mycobacteria. I. Multicenter prevalence study in cystic fibrosis, Am J Respir Crit Care Med, vol.167, pp.828-834

R. A. Floto, US cystic fibrosis foundation and European cystic fibrosis society consensus recommendations for the management of non-tuberculous mycobacteria in individuals with cystic fibrosis: Executive summary, Thorax, vol.71, pp.88-90, 2016.

E. D. Chan and M. D. Iseman, Underlying host risk factors for nontuberculous mycobacterial lung disease, Semin Respir Crit Care Med, vol.34, pp.110-123, 2013.

I. K. Park and K. N. Olivier, Nontuberculous mycobacteria in cystic fibrosis and noncystic fibrosis bronchiectasis, Semin Respir Crit Care Med, vol.36, pp.217-224, 2015.

G. Lamichhane, S. Tyagi, and W. R. Bishai, Designer arrays for defined mutant analysis to detect genes essential for survival of Mycobacterium tuberculosis in mouse lungs, Infect Immun, vol.73, pp.2533-2540, 2005.

R. M. Wells, Discovery of a siderophore export system essential for virulence of Mycobacterium tuberculosis, PLoS Pathog, vol.9, p.1003120, 2013.

M. Jain and J. S. Cox, Interaction between polyketide synthase and transporter suggests coupled synthesis and export of virulence lipid in M. tuberculosis, PLoS Pathog, vol.1, p.2, 2005.

S. E. Converse, MmpL8 is required for sulfolipid-1 biosynthesis and Mycobacterium tuberculosis virulence, Proc Natl Acad Sci, vol.100, pp.6121-6126, 2003.

S. A. Pacheco, F. Hsu, K. M. Powers, and G. E. Purdy, MmpL11 protein transports mycolic acid-containing lipids to the mycobacterial cell wall and contributes to biofilm formation in Mycobacterium smegmatis, J Biol Chem, vol.288, pp.24213-24222, 2013.

J. M. Belardinelli, Biosynthesis and translocation of unsulfated acyltrehaloses in Mycobacterium tuberculosis, J Biol Chem, vol.289, pp.27952-27965, 2014.

E. C. Boritsch, recombination-mediated surface remodelling in Mycobacterium tuberculosis emergence, Nat Microbiol, vol.1, p.15019, 2016.
URL : https://hal.archives-ouvertes.fr/pasteur-01265519

J. Briffotaux, W. Huang, X. Wang, and B. Gicquel, MmpS5/MmpL5 as an efflux pump in Mycobacterium species, Tuberculosis (Edinb), vol.107, pp.13-19, 2017.

C. Astarie-dequeker, Phthiocerol dimycocerosates of M. tuberculosis participate in macrophage invasion by inducing changes in the organization of plasma membrane lipids, PLoS Pathog, vol.5, p.1000289, 2009.

J. Quigley, The cell wall lipid PDIM contributes to phagosomal escape and host cell exit of Mycobacterium tuberculosis, MBio, vol.8, pp.148-165, 2017.

J. Augenstreich, ESX-1 and phthiocerol dimycocerosates of Mycobacterium tuberculosis act in concert to cause phagosomal rupture and host cell apoptosis, Cell Microbiol, vol.19, p.12726, 2017.

T. J. Rowbotham, Isolation of Legionella pneumophila from clinical specimens via amoebae, and the interaction of those and other isolates with amoebae, J Clin Pathol, vol.36, pp.978-986, 1983.

E. Quevillon, InterProScan: Protein domains identifier, Nucleic Acids Res, vol.33, pp.116-120, 2005.

L. Guy, J. R. Kultima, and S. Andersson, genoPlotR: Comparative gene and genome visualization in R, Bioinformatics, vol.26, pp.2334-2335, 2010.

L. Moigne and V. , MgtC as a host-induced factor and vaccine candidate against Mycobacterium abscessus infection, Infect Immun, vol.84, pp.2895-2903, 2016.

J. C. Kessel and G. F. Hatfull, Recombineering in Mycobacterium tuberculosis, Nat Methods, vol.4, pp.147-152, 2007.

G. S. Besra, Preparation of cell-wall fractions from Mycobacteria. Mycobacteria Protocols, vol.101, pp.91-108, 1998.

J. P. Kamerling, G. J. Gerwig, J. F. Vliegenthart, and J. R. Clamp, Characterization by gas-liquid chromatography-mass spectrometry and proton-magnetic-resonance spectroscopy of pertrimethylsilyl methyl glycosides obtained in the methanolysis of glycoproteins and glycopeptides, Biochem J, vol.151, pp.491-495, 1975.

J. Hytönen, S. Haataja, and J. Finne, Use of flow cytometry for the adhesion analysis of Streptococcus pyogenes mutant strains to epithelial cells: Investigation of the possible role of surface pullulanase and cysteine protease, and the transcriptional regulator Rgg, BMC Microbiol, vol.6, p.18, 2006.

R. Simeone, Cytosolic access of Mycobacterium tuberculosis: Critical impact of phagosomal acidification control and demonstration of occurrence in vivo, PLoS Pathog, vol.11, p.1004650, 2015.

M. I. Gröschel, Recombinant BCG expressing ESX-1 of Mycobacterium marinum combines low virulence with cytosolic immune signaling and improved TB protection, Cell Rep, vol.18, pp.2752-2765, 2017.

M. Hagedorn, K. H. Rohde, D. G. Russell, and T. Soldati, Infection by tubercular mycobacteria is spread by nonlytic ejection from their amoeba hosts, Science, vol.323, pp.1729-1733, 2009.

E. C. Boritsch, A glimpse into the past and predictions for the future: The molecular evolution of the tuberculosis agent, Mol Microbiol, vol.93, pp.835-852, 2014.

T. J. Rowbotham, Preliminary report on the pathogenicity of Legionella pneumophila for freshwater and soil amoebae, J Clin Pathol, vol.33, pp.1179-1183, 1980.

D. Corsaro, R. Michel, J. Walochnik, K. Müller, and G. Greub, Saccamoeba lacustris, sp. nov. (Amoebozoa: Lobosea: Hartmannellidae), a new lobose amoeba, parasitized by the novel chlamydia 'Candidatus Metachlamydia lacustris' (Chlamydiae: Parachlamydiaceae), Eur J Protistol, vol.46, pp.86-95, 2010.

T. R. Fritsche, R. K. Gautom, S. Seyedirashti, D. L. Bergeron, and T. D. Lindquist, Occurrence of bacterial endosymbionts in Acanthamoeba spp. isolated from corneal and environmental specimens and contact lenses, J Clin Microbiol, vol.31, pp.1122-1126, 1993.

A. Croxatto, V. Murset, B. Chassot, and G. Greub, Early expression of the type III secretion system of Parachlamydia acanthamoebae during a replicative cycle within its natural host cell Acanthamoeba castellanii, vol.69, pp.159-175, 2013.

G. Greub and D. Raoult, Microorganisms resistant to free-living amoebae, Clin Microbiol Rev, vol.17, pp.413-433, 2004.

E. M. Weerdenburg, Genome-wide transposon mutagenesis indicates that Mycobacterium marinum customizes its virulence mechanisms for survival and replication in different hosts, Infect Immun, vol.83, pp.1778-1788, 2015.

J. D. Cirillo, S. Falkow, L. S. Tompkins, and L. E. Bermudez, Interaction of Mycobacterium avium with environmental amoebae enhances virulence, Infect Immun, vol.65, pp.3759-3767, 1997.

R. J. Wallace, B. A. Brown, and D. E. Griffith, Nosocomial outbreaks/pseudo-outbreaks caused by nontuberculous mycobacteria, Annu Rev Microbiol, vol.52, pp.453-490, 1998.

R. S. Duarte, Epidemic of postsurgical infections caused by Mycobacterium massiliense, J Clin Microbiol, vol.47, pp.2149-2155, 2009.

S. C. Leão, Epidemic of surgical-site infections by a single clone of rapidly growing mycobacteria in Brazil, Future Microbiol, vol.5, pp.971-980, 2010.

K. N. Olivier, Nontuberculous Mycobacteria in Cystic Fibrosis Study Group (2003) Nontuberculous mycobacteria. I: Multicenter prevalence study in cystic fibrosis, Am J Respir Crit Care Med, vol.167, pp.828-834

A. Roux, Multicenter study of prevalence of nontuberculous mycobacteria in patients with cystic fibrosis in France, J Clin Microbiol, vol.47, pp.4124-4128, 2009.
URL : https://hal.archives-ouvertes.fr/hal-01857711

D. E. Griffith, W. M. Girard, R. J. Wallace, and J. , Clinical features of pulmonary disease caused by rapidly growing mycobacteria. An analysis of 154 patients, Am Rev Respir Dis, vol.147, pp.1271-1278, 1993.

T. Qvist, Comparing the harmful effects of nontuberculous mycobacteria and gram negative bacteria on lung function in patients with cystic fibrosis, J Cyst Fibros, vol.15, pp.380-385, 2016.

B. E. Jönsson, Molecular epidemiology of Mycobacterium abscessus, with focus on cystic fibrosis, J Clin Microbiol, vol.45, pp.1497-1504, 2007.

J. M. Bryant, Emergence and spread of a human-transmissible multidrugresistant nontuberculous Mycobacterium, Science, vol.354, pp.751-757, 2016.

A. R. Cullen, C. L. Cannon, E. J. Mark, and A. A. Colin, Mycobacterium abscessus infection in cystic fibrosis. Colonization or infection?, Am J Respir Crit Care Med, vol.161, pp.641-645, 2000.

K. M. Kreutzfeldt, Molecular longitudinal tracking of Mycobacterium abscessus spp. during chronic infection of the human lung, PLoS One, vol.8, p.63237, 2013.
DOI : 10.1371/journal.pone.0063237
URL : https://journals.plos.org/plosone/article/file?id=10.1371/journal.pone.0063237&type=printable

E. Catherinot, Acute respiratory failure involving an R variant of Mycobacterium abscessus, J Clin Microbiol, vol.47, pp.271-274, 2009.

A. Bernut, Mycobacterium abscessus cording prevents phagocytosis and promotes abscess formation, Proc Natl Acad Sci, vol.111, pp.943-952, 2014.
DOI : 10.1073/pnas.1321390111
URL : http://www.pnas.org/content/111/10/E943.full.pdf

E. Catherinot, Hypervirulence of a rough variant of the Mycobacterium abscessus type strain, Infect Immun, vol.75, pp.1055-1058, 2007.

A. Roux, Overexpression of proinflammatory TLR-2-signalling lipoproteins in hypervirulent mycobacterial variants, Cell Microbiol, vol.13, pp.692-704, 2011.

F. Ripoll, Non mycobacterial virulence genes in the genome of the emerging pathogen Mycobacterium abscessus, PLoS One, vol.4, p.5660, 2009.

J. O. Falkinham, E. D. Hilborn, M. J. Arduino, A. Pruden, and M. A. Edwards, Epidemiology and ecology of opportunistic premise plumbing pathogens: Legionella pneumophila, Mycobacterium avium, and Pseudomonas aeruginosa, Environ Health Perspect, vol.123, pp.749-758, 2015.

E. Cateau, Stenotrophomonas maltophilia and Vermamoeba vermiformis relationships: Bacterial multiplication and protection in amoebal-derived structures, Res Microbiol, vol.165, pp.847-851, 2014.
URL : https://hal.archives-ouvertes.fr/hal-01427338

L. Moigne and V. , MgtC as a host-induced factor and vaccine candidate against Mycobacterium abscessus infection, Infect Immun, vol.84, pp.2895-2903, 2016.

E. J. Rubin, In vivo transposition of mariner-based elements in enteric bacteria and mycobacteria, Proc Natl Acad Sci, vol.96, pp.1645-1650, 1999.

A. Roux, The distinct fate of smooth and rough Mycobacterium abscessus variants inside macrophages, Open Biol, vol.6, p.160185, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01438481

E. Dumas, Mycobacterial pan-genome analysis suggests important role of plasmids in the radiation of type VII secretion systems, Genome Biol Evol, vol.8, pp.387-402, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01291528

M. Unnikrishnan, C. Constantinidou, T. Palmer, and M. J. Pallen, The enigmatic Esx proteins: Looking beyond mycobacteria, Trends Microbiol, vol.25, pp.192-204, 2017.

M. Zhang, EspI regulates the ESX-1 secretion system in response to ATP levels in Mycobacterium tuberculosis, Mol Microbiol, vol.93, pp.1057-1065, 2014.

S. Raman, Mycobacterium tuberculosis SigM positively regulates Esx secreted protein and nonribosomal peptide synthetase genes and down regulates virulence-associated surface lipid synthesis, J Bacteriol, vol.188, pp.8460-8468, 2006.

J. A. Armstrong and P. D. Hart, Response of cultured macrophages to Mycobacterium tuberculosis, with observations on fusion of lysosomes with phagosomes, J Exp Med, vol.134, pp.713-740, 1971.

S. Sturgill-koszycki, Lack of acidification in Mycobacterium phagosomes produced by exclusion of the vesicular proton-ATPase, Science, vol.263, pp.678-681, 1994.

R. Simeone, D. Bottai, W. Frigui, L. Majlessi, and R. Brosch, ESX/type VII secretion systems of mycobacteria: Insights into evolution, pathogenicity and protection, Tuberculosis (Edinb), vol.95, pp.150-154, 2015.

R. Simeone, Cytosolic access of Mycobacterium tuberculosis: Critical impact of phagosomal acidification control and demonstration of occurrence in vivo, PLoS Pathog, vol.11, p.1004650, 2015.

D. Soroka, Characterization of broad-spectrum Mycobacterium abscessus class A ?-lactamase, J Antimicrob Chemother, vol.69, pp.691-696, 2014.

J. Augenstreich, ESX-1 and phthiocerol dimycocerosates of Mycobacterium tuberculosis act in concert to cause phagosomal rupture and host cell apoptosis, Cell Microbiol, vol.19, p.12726, 2017.

L. Majlessi and R. Brosch, Mycobacterium tuberculosis meets the cytosol: The role of cGAS in anti-mycobacterial immunity, Cell Host Microbe, vol.17, pp.733-735, 2015.

R. Wassermann, Mycobacterium tuberculosis differentially Activates cGAS-and inflammasome-dependent intracellular immune responses through ESX-1, Cell Host Microbe, vol.17, pp.799-810, 2015.

M. I. Gröschel, Recombinant BCG expressing ESX-1 of Mycobacterium marinum combines low virulence with cytosolic immune signaling and improved TB protection, Cell Rep, vol.18, pp.2752-2765, 2017.

T. Adékambi, B. Salah, S. Khlif, M. Raoult, D. Drancourt et al., Survival of environmental mycobacteria in Acanthamoeba polyphaga, Appl Environ Microbiol, vol.72, pp.5974-5981, 2006.

I. Paz, Galectin-3, a marker for vacuole lysis by invasive pathogens, Cell Microbiol, vol.12, pp.530-544, 2010.
URL : https://hal.archives-ouvertes.fr/hal-00486248

T. Thurston, M. P. Wandel, N. Von-muhlinen, A. Foeglein, and F. Randow, Galectin 8 targets damaged vesicles for autophagy to defend cells against bacterial invasion, Nature, vol.482, pp.414-418, 2012.

R. Simeone, Phagosomal rupture by Mycobacterium tuberculosis results in toxicity and host cell death, PLoS Pathog, vol.8, p.1002507, 2012.
URL : https://hal.archives-ouvertes.fr/pasteur-01899479

. Laencina, PNAS Early Edition |, vol.9, p.10

Y. S. Kim, Mycobacterium abscessus ESX-3 plays an important role in host inflammatory and pathological responses during infection, Microbes Infect, vol.19, pp.5-17, 2017.

T. A. Gray, Intercellular communication and conjugation are mediated by ESX secretion systems in mycobacteria, Science, vol.354, pp.347-350, 2016.

E. Houben, Composition of the type VII secretion system membrane complex, Mol Microbiol, vol.86, pp.472-484, 2012.

A. M. Abdallah, Type VII secretion-Mycobacteria show the way, Nat Rev Microbiol, vol.5, pp.883-891, 2007.

K. Beckham, Structure of the mycobacterial ESX-5 type VII secretion system membrane complex by single-particle analysis, Nat Microbiol, vol.2, p.17047, 2017.

A. M. Abdallah, PPE and PE_PGRS proteins of Mycobacterium marinum are transported via the type VII secretion system ESX-5, Mol Microbiol, vol.73, pp.329-340, 2009.

V. K. Singh, A unique PE_PGRS protein inhibiting host cell cytosolic defenses and sustaining full virulence of Mycobacterium marinum in multiple hosts, Cell Microbiol, vol.18, pp.1489-1507, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01453293

A. Tanne, A murine DC-SIGN homologue contributes to early host defense against Mycobacterium tuberculosis, J Exp Med, vol.206, pp.2205-2220, 2009.
DOI : 10.1084/jem.20090188
URL : http://jem.rupress.org/content/206/10/2205.full.pdf

H. Medjahed and A. K. Singh, Genetic manipulation of Mycobacterium abscessus, Curr Protoc Microbiol Chapter, 2010.

P. Poullet, S. Carpentier, and E. Barillot, ) myProMS, a web server for management and validation of mass spectrometry-based proteomic data, Proteomics, vol.7, pp.2553-2556, 2007.

G. S. Besra, Preparation of cell-wall fractions from mycobacteria, Mycobacteria Protocols (Humana, pp.91-108, 1998.

T. Qvist, D. Taylor-robinson, and E. Waldmann, Comparing the harmful effects of nontuberculous mycobacteria and Gram negative bacteria on lung function in patients with cystic fibrosis, J Cyst Fibros, vol.15, pp.380-385, 2016.

A. R. Cullen, C. L. Cannon, and E. J. Mark, Mycobacterium abscessus infection in cystic fibrosis. Colonization or infection?, Am J Respir Crit Care Med, vol.161, pp.641-646, 2000.

J. M. Bryant, D. M. Grogono, and D. Greaves, Wholegenome sequencing to identify transmission of Mycobacterium abscessus between patients with cystic fibrosis: a retrospective cohort study, Lancet, vol.381, pp.1551-60, 2013.

F. Ripoll, S. Pasek, and C. Schenowitz, Non mycobacterial virulence genes in the genome of the emerging pathogen Mycobacterium abscessus, PLoS One, vol.4, p.5660, 2009.

N. Bakala, J. C. Goma, V. Moigne, . Le, and N. Soismier, Mycobacterium abscessus phospholipase C expression is induced during coculture within amoebae and enhances M. abscessus virulence in mice, Infect Immun, vol.83, pp.780-91, 2015.

J. D. Cirillo, S. Falkow, and L. S. Tompkins, Interaction of Mycobacterium avium with environmental amoebae enhances virulence, Infect Immun, vol.65, pp.3759-67, 1997.

A. Bernut, J. L. Herrmann, and G. Lutfalla, Les cordes mycobactériennes : un nouveau moyen d'échappement au système immunitaire ?, Med Sci, vol.30, pp.499-522, 2014.
DOI : 10.1051/medsci/20143005008
URL : https://www.medecinesciences.org/articles/medsci/pdf/2014/06/medsci20143005p499.pdf

A. Roux, A. Viljoen, and A. Bah, The distinct fate of smooth and rough Mycobacterium abscessus variants inside macrophages, Open Biol, vol.6, p.160185, 2016.
URL : https://hal.archives-ouvertes.fr/hal-01438481

M. I. Groschel, F. Sayes, and R. Simeone, ESX secretion systems: mycobacterial evolution to counter host immunity, Nat Rev Microbiol, vol.14, pp.677-91, 2016.

L. Laencina, V. Dubois, V. Moigne, and . Le, Identification of genes required for Mycobacterium abscessus growth in vivo with a prominent role of the ESX-4 locus, Proc Natl Acad Sci, vol.115, pp.1002-1013, 2018.
URL : https://hal.archives-ouvertes.fr/pasteur-02046027