147 articles – 175 Notices  [english version]
Fiche concise Articles dans des revues avec comité de lecture
Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.
Pourceau G. et al
ChemBioChem 12, 13 (2011) 2071-80 - http://hal.archives-ouvertes.fr/hal-00691511
Gwladys Pourceau1, Yann Chevolot2, Alice Goudot2, Fabienne Giroux3, Albert Meyer1, Vincent Moulés3, Bruno Lina3, Samy Cecioni4, Sébastien Vidal4, Hai Yu5, Xi Chen5, Olivier Ferraris3, Jean-Pierre Praly4, Eliane Souteyrand2, Jean-Jacques Vasseur1, François Morvan1
1 :  IBMM - Institut des Biomolécules Max Mousseron
CNRS : UMR5247 – Université Montpellier I – Université Montpellier II - Sciences et techniques
Faculté de pharmacie 15, Avenue Charles Flahault 34060 MONTPELLIER CEDEX 2
France
2 :  INL - Institut des nanotechnologies de Lyon - Site d'Ecully
CNRS : UMR5270 – Université Claude Bernard - Lyon I – Institut National des Sciences Appliquées [INSA] - Lyon – Ecole Centrale de Lyon
bat. 7 36 Av Guy de Collongue - 163 69131 ECULLY CEDEX
France
3 :  VirPath - Virologie et Pathologie Humaine
CNRS : FRE3011 – Université Claude Bernard - Lyon I – École Normale Supérieure (ENS) - Lyon
Faculté de Médecine Lyon RTH Laennec 7 rue Guillaume Paradin 69372 LYON CEDEX 08
France
4 :  ICBMS - Institut de Chimie et Biochimie Moléculaires et Supramoléculaires
CNRS : UMR5246 – Université Claude Bernard - Lyon I – Institut National des Sciences Appliquées [INSA] - Lyon – École Supérieure Chimie Physique Électronique de Lyon
Bâtiment CPE 43, Bld du 11 novembre 1918 69622 VILLEURBANNE CEDEX
France
5 :  University of California
University of California
États-Unis
Chimie/Chimie organique
21739555
Measurement of enzymatic activity and specificity of human and avian influenza neuraminidases from whole virus by glycoarray and MALDI-TOF mass spectrometry.
Influenza neuraminidases hydrolyze the ketosidic linkage between N-acetylneuraminic acid and its adjacent galactose residue in sialosides. This enzyme is a tetrameric protein that plays a critical role in the release of progeny virions. Several methods have been described for the determination of neuraminidase activity, usually based on colorimetric, fluorescent, or chemiluminescent detection. However, only a few of these tests allow discrimination of the sialyl-linkage specificity (i.e., α2-3- versus α2-6-linked sialyllactosides) of the neuraminidase. Herein we report a glycoarray-based assay and a MALDI-TOF study for assessing the activity and specificity of two influenza neuraminidases on whole viruses. The human A(H3N2) and avian A(H5N2) neuraminidase activities were investigated. The results from both approaches demonstrated that α2-3 sialyllactoside was a better substrate than α2-6 sialyllactoside for both viruses and that H5N2 virus had a lower hydrolytic activity than H3N2.
Anglais

10.1002/cbic.201100128
ChemBioChem
internationale
05/09/2011
12
13
2071-80

Equipe : Chimie Organique 2-Glycochimie (CO2GLYCO)