A neutralizing antibody Fab-influenza haemagglutinin complex with an unprecedented 2 : 1 stoichiometry: characterization and crystallization

Authors
Gigant, B Barbey-Martin, C Bizebard, T Fleury, D Daniels, R Skehel, JJ Knossow, M
Citation
B. Gigant et al., A neutralizing antibody Fab-influenza haemagglutinin complex with an unprecedented 2 : 1 stoichiometry: characterization and crystallization, ACT CRYST D, 56, 2000, pp. 1067-1069
Citations number
17
Categorie Soggetti
Chemistry & Analysis
Journal title
ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY
ISSN journal
09074449 → ACNP
Volume
56
Year of publication
2000
Part
8
Pages
1067 - 1069
Database
ISI
SICI code
0907-4449(200008)56:<1067:ANAFHC>2.0.ZU;2-C
Abstract
The haemagglutinin HA is a trimer of identical subunits and is the more abu ndant viral surface glycoprotein of the influenza virus. It is the target o f antibodies that neutralize viral infectivity. Antibodies that bind to HA with 3:1 and 1:1 stoichiometries have been identified. Here, an antibody wh ose Fab binds to HA with an unprecedented 2:1 Fab:HA stoichiometry is chara cterized. The complex has been crystallized and synchrotron data to 3.5 Ang strom resolution have been collected. Molecular replacement confirms the st oichiometry of the complex.