期刊
VIROLOGY
卷 456, 期 -, 页码 179-187出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.virol.2014.03.008
关键词
Avian influenza virus; H5N1 influenza virus; Haemagglutinin; Receptor specificity; Receptor binding; Biolayer interferometry; Haemagglutinin crystal structure
类别
资金
- Biotechnology and Biological Sciences Research Council [BB/E010806]
- Medical Research Council [U117584222, U117570592, U117585868, U117512723]
- BBSRC [BB/E010806/1] Funding Source: UKRI
- MRC [MC_U117512723, MC_U117585868, MC_U117584222, G0600522] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/E010806/1] Funding Source: researchfish
- Medical Research Council [MC_U117585868, MC_U117512723, G0600522, MC_U117584222] Funding Source: researchfish
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, Delta 133/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. (C) 2014 The Authors. Published by Elsevier Inc.
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