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