Structure of the influenza virus haemagglutinin complexed with its receptor, sialic acid.
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.
Weis
W
W
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Brown
J H
JH
Cusack
S
S
Paulson
J C
JC
Skehel
J J
JJ
Wiley
D C
DC
D000906:Antibodies / Q000378:metabolism; D000998:Antiviral Agents / Q000378:metabolism; D001665:Binding Sites; D001666:Binding Sites, Antibody; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D019158:N-Acetylneuraminic Acid; D009975:Orthomyxoviridae / Q000032:analysis*; D011485:Protein Binding; D011487:Protein Conformation; D011991:Receptors, Virus / Q000276:immunology / Q000378:metabolism*; D012794:Sialic Acids / Q000378:metabolism*
D000906:Antibodies; D000998:Antiviral Agents; D019267:Hemagglutinin Glycoproteins, Influenza Virus; D006389:Hemagglutinins, Viral; D011991:Receptors, Virus; D012794:Sialic Acids; D019158:N-Acetylneuraminic Acid