Abstract
The three-dimensional structures of influenza virus haemagglutinins complexed with cell receptor analogues show sialic acids bound to a pocket of conserved amino acids surrounded by antibody-binding sites. Sialic acid fills the conserved pocket, demonstrating that it is the influenza virus receptor. The proximity of the antibody-binding sites suggests that antibodies neutralize virus infectivity by preventing virus-to-cell binding. The structures suggest approaches to the design of anti-viral drugs that could block attachment of viruses to cells.
Publication types
-
Research Support, Non-U.S. Gov't
-
Research Support, U.S. Gov't, Non-P.H.S.
-
Research Support, U.S. Gov't, P.H.S.
MeSH terms
-
Antibodies / metabolism
-
Antiviral Agents / metabolism
-
Binding Sites
-
Binding Sites, Antibody
-
Hemagglutinin Glycoproteins, Influenza Virus
-
Hemagglutinins, Viral / genetics
-
Hemagglutinins, Viral / metabolism*
-
Models, Molecular
-
N-Acetylneuraminic Acid
-
Orthomyxoviridae / analysis*
-
Protein Binding
-
Protein Conformation
-
Receptors, Virus / immunology
-
Receptors, Virus / metabolism*
-
Sialic Acids / metabolism*
Substances
-
Antibodies
-
Antiviral Agents
-
Hemagglutinin Glycoproteins, Influenza Virus
-
Hemagglutinins, Viral
-
Receptors, Virus
-
Sialic Acids
-
N-Acetylneuraminic Acid