An Antibody That Prevents the Hemagglutinin Low pH Fusogenic Transition

We have determined the structure of a complex of influenza hemagglutinin (HA) with an antibody that binds simultaneously to the membrane-distal domains of two HA monomers, effectively cross-linking them. The antibody prevents the low pH structural transition of HA that is required for its membrane f...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2002-03, Vol.294 (1), p.70-74
Main Authors: Barbey-Martin, C, Gigant, B, Bizebard, T, Calder, L.J, Wharton, S.A, Skehel, J.J, Knossow, M
Format: Article
Language:English
Subjects:
Antibodies, Viral - immunology
antibody
Antibody Affinity
Biochemistry, Molecular Biology
hemagglutinin
Hemagglutinin Glycoproteins, Influenza Virus - chemistry
Hemagglutinin Glycoproteins, Influenza Virus - immunology
Hemagglutinin Glycoproteins, Influenza Virus - physiology
Hydrogen-Ion Concentration
Immunoglobulin Fab Fragments - immunology
influenza
Influenza virus
Life Sciences
Membrane Fusion
Microbiology and Parasitology
Models, Molecular
Orthomyxoviridae - physiology
Protein Conformation
Structural Biology
structure
Virology
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Summary:We have determined the structure of a complex of influenza hemagglutinin (HA) with an antibody that binds simultaneously to the membrane-distal domains of two HA monomers, effectively cross-linking them. The antibody prevents the low pH structural transition of HA that is required for its membrane fusion activity, providing evidence that a rearrangement of HA membrane-distal domains is an essential component of the transition.
ISSN:0042-6822
1096-0341
DOI:10.1006/viro.2001.1320