Enhanced human receptor binding by H5 haemagglutinins
Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved..
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.
| Medienart: |
E-Artikel |
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| Erscheinungsjahr: |
2014 |
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| Erschienen: |
2014 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:456-457 |
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| Enthalten in: |
Virology - 456-457(2014) vom: 07. Mai, Seite 179-87 |
| Sprache: |
Englisch |
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| Beteiligte Personen: |
Xiong, Xiaoli [VerfasserIn] |
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| Links: |
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| Anmerkungen: |
Date Completed 21.07.2014 Date Revised 29.01.2022 published: Print-Electronic Citation Status MEDLINE |
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| doi: |
10.1016/j.virol.2014.03.008 |
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| funding: |
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| Förderinstitution / Projekttitel: |
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| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved. | ||
| 520 | |a 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 | ||
| 650 | 4 | |a Comparative Study | |
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Avian influenza virus | |
| 650 | 4 | |a Biolayer interferometry | |
| 650 | 4 | |a H5N1 influenza virus | |
| 650 | 4 | |a Haemagglutinin | |
| 650 | 4 | |a Haemagglutinin crystal structure | |
| 650 | 4 | |a Receptor binding | |
| 650 | 4 | |a Receptor specificity | |
| 650 | 7 | |a Hemagglutinin Glycoproteins, Influenza Virus |2 NLM | |
| 650 | 7 | |a Receptors, Virus |2 NLM | |
| 650 | 7 | |a hemagglutinin, avian influenza A virus |2 NLM | |
| 700 | 1 | |a Xiao, Haixia |e verfasserin |4 aut | |
| 700 | 1 | |a Martin, Stephen R |e verfasserin |4 aut | |
| 700 | 1 | |a Coombs, Peter J |e verfasserin |4 aut | |
| 700 | 1 | |a Liu, Junfeng |e verfasserin |4 aut | |
| 700 | 1 | |a Collins, Patrick J |e verfasserin |4 aut | |
| 700 | 1 | |a Vachieri, Sebastien G |e verfasserin |4 aut | |
| 700 | 1 | |a Walker, Philip A |e verfasserin |4 aut | |
| 700 | 1 | |a Lin, Yi Pu |e verfasserin |4 aut | |
| 700 | 1 | |a McCauley, John W |e verfasserin |4 aut | |
| 700 | 1 | |a Gamblin, Steven J |e verfasserin |4 aut | |
| 700 | 1 | |a Skehel, John J |e verfasserin |4 aut | |
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