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 fusion activity, providing evidence that a rearrangement of HA membrane-distal domains is an essential component of the transition.
Barbey-Martin
C
C
Laboratoire d'Enzymologie et Biochimie Structurales, UPR 9063 CNRS, Bât. 34, CNRS, 91198 Gif-sur-Yvette Cedex, France.
Gigant
B
B
Bizebard
T
T
Calder
L J
LJ
Wharton
S A
SA
Skehel
J J
JJ
Knossow
M
M
D000914:Antibodies, Viral / Q000276:immunology; D000915:Antibody Affinity; D019267:Hemagglutinin Glycoproteins, Influenza Virus / Q000737:chemistry / Q000276:immunology* / Q000502:physiology; D006863:Hydrogen-Ion Concentration; D007140:Immunoglobulin Fab Fragments / Q000276:immunology*; D008561:Membrane Fusion; D008958:Models, Molecular; D009975:Orthomyxoviridae / Q000502:physiology*; D011487:Protein Conformation
D000914:Antibodies, Viral; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D007140:Immunoglobulin Fab Fragments