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Enhanced human receptor binding by H5 haemagglutinins

DOI: 10.1016/j.virol.2014.03.008 DOI Help
PMID: 24889237 PMID Help

Authors: Xiaoli Xiong (MRC National Institute for Medical Research) , Haixia Xiao (MRC National Institute for Medical Research) , Stephen R. Martin (MRC National Institute for Medical Research) , Peter J. Coombs (MRC National Institute for Medical Research) , Junfeng Liu (MRC National Institute for Medical Research) , Patrick Collins (MRC National Institute for Medical Research) , Sebastien Vachieri (MRC Medical Research Council, National Institute for Medical Research) , Phil Walker (MRC National Institute for Medical Research) , Yi Pu Lin (MRC National Institute for Medical Research) , John W. Mccauley (MRC National Institute for Medical Research) , Steven Gamblin (National Institute for Medical Research, Medical Research Council) , John J. Skehel (National Institute for Medical Research, Medical Research Council)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Virology , VOL 456 , PAGES 179 - 187

State: Published (Approved)
Published: May 2014
Diamond Proposal Number(s): 7707

Open Access Open Access

Abstract: Mutant H5N1 influenza viruses have been isolated from humans that have increased human receptor avidity. We have compared the receptor binding properties of these mutants with those of wild-type viruses, and determined the structures of their haemagglutinins in complex with receptor analogues. Mutants from Vietnam bind tighter to human receptor by acquiring basic residues near the receptor binding site. They bind more weakly to avian receptor because they lack specific interactions between Asn-186 and Gln-226. In contrast, a double mutant, Δ133/Ile155Thr, isolated in Egypt has greater avidity for human receptor while retaining wild-type avidity for avian receptor. Despite these increases in human receptor binding, none of the mutants prefers human receptor, unlike aerosol transmissible H5N1 viruses. Nevertheless, mutants with high avidity for both human and avian receptors may be intermediates in the evolution of H5N1 viruses that could infect both humans and poultry.

Journal Keywords: Birds; Crystallography; X-Ray; Hemagglutinin; Influenza; Humans; Influenza; H5N1; Influenza; Influenza; Human; Models; Molecular; Protein; Receptors; Virus

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography , I04-1-Macromolecular Crystallography (fixed wavelength) , I04-Macromolecular Crystallography

Added On: 22/09/2014 13:37

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