Enhanced human receptor binding by H5 haemagglutinins
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 analogu...
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| Veröffentlicht in: | Virology (New York, N.Y.) N.Y.), 2014-05, Vol.456 (100), p.179-187 |
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| creator | Xiong, Xiaoli Xiao, Haixia Martin, Stephen R Coombs, Peter J Liu, Junfeng Collins, Patrick J Vachieri, Sebastien G Walker, Philip A Lin, Yi Pu McCauley, John W Gamblin, Steven J Skehel, John J |
| description | 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. |
| doi_str_mv | 10.1016/j.virol.2014.03.008 |
| format | Article |
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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.</description><identifier>ISSN: 0042-6822</identifier><identifier>EISSN: 1096-0341</identifier><identifier>DOI: 10.1016/j.virol.2014.03.008</identifier><identifier>PMID: 24889237</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; Avian influenza virus ; Biolayer interferometry ; Birds ; Crystallography, X-Ray ; H5N1 influenza virus ; Haemagglutinin ; Haemagglutinin crystal structure ; Hemagglutinin Glycoproteins, Influenza Virus - chemistry ; Hemagglutinin Glycoproteins, Influenza Virus - metabolism ; Humans ; Infectious Disease ; Influenza A Virus, H5N1 Subtype - isolation & purification ; Influenza A Virus, H5N1 Subtype - physiology ; Influenza in Birds - virology ; Influenza, Human - virology ; Models, Molecular ; Protein Binding ; Protein Conformation ; Receptor binding ; Receptor specificity ; Receptors, Virus - chemistry ; Receptors, Virus - metabolism</subject><ispartof>Virology (New York, N.Y.), 2014-05, Vol.456 (100), p.179-187</ispartof><rights>The Authors</rights><rights>2014 The Authors</rights><rights>Copyright © 2014 The Authors. 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All rights reserved.</rights><rights>2014 The Authors 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c547t-d4a6bbe9183549d9407e1ba6273845b282ff78f979be573fe3f0cf9830ced1ac3</citedby><cites>FETCH-LOGICAL-c547t-d4a6bbe9183549d9407e1ba6273845b282ff78f979be573fe3f0cf9830ced1ac3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0042682214000907$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,776,780,881,3536,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24889237$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xiong, Xiaoli</creatorcontrib><creatorcontrib>Xiao, Haixia</creatorcontrib><creatorcontrib>Martin, Stephen R</creatorcontrib><creatorcontrib>Coombs, Peter J</creatorcontrib><creatorcontrib>Liu, Junfeng</creatorcontrib><creatorcontrib>Collins, Patrick J</creatorcontrib><creatorcontrib>Vachieri, Sebastien G</creatorcontrib><creatorcontrib>Walker, Philip A</creatorcontrib><creatorcontrib>Lin, Yi Pu</creatorcontrib><creatorcontrib>McCauley, John W</creatorcontrib><creatorcontrib>Gamblin, Steven J</creatorcontrib><creatorcontrib>Skehel, John J</creatorcontrib><title>Enhanced human receptor binding by H5 haemagglutinins</title><title>Virology (New York, N.Y.)</title><addtitle>Virology</addtitle><description>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.</description><subject>Animals</subject><subject>Avian influenza virus</subject><subject>Biolayer interferometry</subject><subject>Birds</subject><subject>Crystallography, X-Ray</subject><subject>H5N1 influenza virus</subject><subject>Haemagglutinin</subject><subject>Haemagglutinin crystal structure</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - chemistry</subject><subject>Hemagglutinin Glycoproteins, Influenza Virus - metabolism</subject><subject>Humans</subject><subject>Infectious Disease</subject><subject>Influenza A Virus, H5N1 Subtype - isolation & purification</subject><subject>Influenza A Virus, H5N1 Subtype - physiology</subject><subject>Influenza in Birds - virology</subject><subject>Influenza, Human - virology</subject><subject>Models, Molecular</subject><subject>Protein Binding</subject><subject>Protein Conformation</subject><subject>Receptor binding</subject><subject>Receptor specificity</subject><subject>Receptors, Virus - chemistry</subject><subject>Receptors, Virus - metabolism</subject><issn>0042-6822</issn><issn>1096-0341</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkk9v1DAQxS0EokvhEyChHLkkjP8ktg9UQlWhSJU4AGfLcSa7XhJnsZOV9tvjsKUCLj1Zlt8bv5nfEPKaQkWBNu_21dHHaagYUFEBrwDUE7KhoJsSuKBPyQZAsLJRjF2QFyntId-lhOfkggmlNONyQ-qbsLPBYVfsltGGIqLDwzzFovWh82FbtKfiti52Fke73Q7L7IMP6SV51tsh4av785J8_3jz7fq2vPvy6fP1h7vS1ULOZSds07aoqeK10J0WIJG2tmGSK1G3TLG-l6rXUrdYS94j78H1WnHIgah1_JJcneselnbEzmGYox3MIfrRxpOZrDf_vgS_M9vpaATUXHGeC7y9LxCnnwum2Yw-ORwGG3BakqG1EAC1yvLHpZwJmbPJLOVnqYtTShH7h0QUzMrG7M1vNmZlY4CbzCa73vzdzIPnD4wseH8WYB7p0WM0yXlc4fiMZTbd5B_54Oo_vxsyLmeHH3jCtJ-WGDItQ01iBszXdT3W7aB5BKBzX78A3yO10w</recordid><startdate>20140501</startdate><enddate>20140501</enddate><creator>Xiong, Xiaoli</creator><creator>Xiao, Haixia</creator><creator>Martin, Stephen R</creator><creator>Coombs, Peter J</creator><creator>Liu, Junfeng</creator><creator>Collins, Patrick J</creator><creator>Vachieri, Sebastien G</creator><creator>Walker, Philip A</creator><creator>Lin, Yi Pu</creator><creator>McCauley, John W</creator><creator>Gamblin, Steven J</creator><creator>Skehel, John J</creator><general>Elsevier Inc</general><general>Academic Press</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7U9</scope><scope>H94</scope><scope>5PM</scope></search><sort><creationdate>20140501</creationdate><title>Enhanced human receptor binding by H5 haemagglutinins</title><author>Xiong, Xiaoli ; 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| ispartof | Virology (New York, N.Y.), 2014-05, Vol.456 (100), p.179-187 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete; EZB-FREE-00999 freely available EZB journals |
| subjects | Animals Avian influenza virus Biolayer interferometry Birds Crystallography, X-Ray H5N1 influenza virus Haemagglutinin Haemagglutinin crystal structure Hemagglutinin Glycoproteins, Influenza Virus - chemistry Hemagglutinin Glycoproteins, Influenza Virus - metabolism Humans Infectious Disease Influenza A Virus, H5N1 Subtype - isolation & purification Influenza A Virus, H5N1 Subtype - physiology Influenza in Birds - virology Influenza, Human - virology Models, Molecular Protein Binding Protein Conformation Receptor binding Receptor specificity Receptors, Virus - chemistry Receptors, Virus - metabolism |
| title | Enhanced human receptor binding by H5 haemagglutinins |
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