tetano
Editor, Senior Moderator
Virology. 2014 May;456-457:179-87. doi: 10.1016/j.virol.2014.03.008. Epub 2014 Apr 12.
Enhanced human receptor binding by H5 haemagglutinins.
Xiong X1, Xiao H1, Martin SR1, Coombs PJ1, Liu J1, Collins PJ1, Vachieri SG1, Walker PA1, Lin YP1, McCauley JW1, Gamblin SJ1, Skehel JJ2.
Author information
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.
Copyright ? 2014 The Authors. Published by Elsevier Inc. All rights reserved.
KEYWORDS:
Avian influenza virus; Biolayer interferometry; H5N1 influenza virus; Haemagglutinin; Haemagglutinin crystal structure; Receptor binding; Receptor specificity
PMID:
24889237
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24889237
Enhanced human receptor binding by H5 haemagglutinins.
Xiong X1, Xiao H1, Martin SR1, Coombs PJ1, Liu J1, Collins PJ1, Vachieri SG1, Walker PA1, Lin YP1, McCauley JW1, Gamblin SJ1, Skehel JJ2.
Author information
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.
Copyright ? 2014 The Authors. Published by Elsevier Inc. All rights reserved.
KEYWORDS:
Avian influenza virus; Biolayer interferometry; H5N1 influenza virus; Haemagglutinin; Haemagglutinin crystal structure; Receptor binding; Receptor specificity
PMID:
24889237
[PubMed - in process]
http://www.ncbi.nlm.nih.gov/pubmed/24889237