Structure of influenza haemagglutinin at the pH of membrane fusion
- 1 September 1994
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 371 (6492), 37-43
- https://doi.org/10.1038/371037a0
Abstract
Low pH induces a conformational change in the influenza virus haemagglutinin, which then mediates fusion of the viral and host cell membranes. The three-dimensional structure of a fragment of the haemagglutinin in this conformation reveals a major refolding of the secondary and tertiary structure of the molecule. The apolar fusion peptide moves at least 100 A to one tip of the molecule. At the other end a helical segment unfolds, a subdomain relocates reversing the chain direction, and part of the structure becomes disordered.This publication has 40 references indexed in Scilit:
- Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activityCell, 1992
- Refinement of the influenza virus hemagglutinin by simulated annealingJournal of Molecular Biology, 1990
- Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin.The Journal of cell biology, 1987
- THE STRUCTURE AND FUNCTION OF THE HEMAGGLUTININ MEMBRANE GLYCOPROTEIN OF INFLUENZA VIRUSAnnual Review of Biochemistry, 1987
- Cell fusion by Semliki Forest, influenza, and vesicular stomatitis viruses.The Journal of cell biology, 1981
- Influenza viruses cause hemolysis and fusion of cellsVirology, 1981
- Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 Å resolutionNature, 1981
- Activation of influenza virus by acidic media causes hemolysis and fusion of erythrocytesFEBS Letters, 1980
- Studies on the primary structure of the influenza virus hemagglutinin.Proceedings of the National Academy of Sciences of the United States of America, 1975
- Crystalline Antigen from the Influenza Virus EnvelopeNature New Biology, 1972