Hemagglutinin structure and activities

DOI: 10.1101/cshperspect.a038638

Authors: Steven J. Gamblin (The Francis Crick Institute) , Sebastien G. Vachieri (The Francis Crick Institute) , Xiaoli Xiong (The Francis Crick Institute) , Jie Zhang (The Francis Crick Institute) , Stephen R. Martin (The Francis Crick Institute) , John J. Skehel (The Francis Crick Institute)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Cold Spring Harbor Perspectives In Medicine

State: Published (Approved)
Published: June 2020
Diamond Proposal Number(s): 9826

Abstract: Hemagglutinins (HAs) are the receptor-binding and membrane fusion glycoproteins of influenza viruses. They recognize sialic acid–containing, cell-surface glycoconjugates as receptors but have limited affinity for them, and, as a consequence, virus attachment to cells requires their interaction with several virus HAs. Receptor-bound virus is transferred into endosomes where membrane fusion by HAs is activated at pH between 5 and 6.5, depending on the strain of virus. Fusion activity requires extensive rearrangements in HA conformation that include extrusion of a buried “fusion peptide” to connect with the endosomal membrane, form a bridge to the virus membrane, and eventually bring both membranes close together. In this review, we give an overview of the structures of the 16 genetically and antigenically distinct subtypes of influenza A HA in relation to these two functions in virus replication and in relation to recognition of HA by antibodies that neutralize infection.

Diamond Keywords: Influenza; Viruses

Subject Areas: Biology and Bio-materials


Instruments: I04-Macromolecular Crystallography

Added On: 02/12/2020 08:37

Discipline Tags:

Pathogens Infectious Diseases Health & Wellbeing Structural biology Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)