Structure of influenza haemagglutinin at the pH of membrane fusion

P A Bullough; F M Hughson; J J Skehel; D C Wiley

doi:10.1038/371037a0

Structure of influenza haemagglutinin at the pH of membrane fusion

Nature. 1994 Sep 1;371(6492):37-43. doi: 10.1038/371037a0.

Authors

P A Bullough¹, F M Hughson, J J Skehel, D C Wiley

Affiliation

¹ Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.

PMID: 8072525
DOI: 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.

Publication types

Research Support, Non-U.S. Gov't
Research Support, U.S. Gov't, P.H.S.

MeSH terms

Amino Acid Sequence
Computer Graphics
Crystallography, X-Ray
Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral / chemistry*
Hemagglutinins, Viral / ultrastructure
Hydrogen-Ion Concentration
Membrane Fusion*
Molecular Sequence Data
Mutation
Orthomyxoviridae / chemistry
Orthomyxoviridae / ultrastructure
Peptide Fragments / chemistry
Protein Conformation
Protein Folding

Substances

Hemagglutinin Glycoproteins, Influenza Virus
Hemagglutinins, Viral
Peptide Fragments