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Enhanced human receptor binding by H5 haemagglutinins
DOI:
10.1016/j.virol.2014.03.008
PMID:
24889237
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

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
Diamond Keywords: Avian Flu; Influenza; Viruses
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
Documents:
1-s2.0-S0042682214000907-main.pdf
Discipline Tags:
Pathogens
Infectious Diseases
Health & Wellbeing
Structural biology
Life Sciences & Biotech
Technical Tags:
Diffraction
Macromolecular Crystallography (MX)