In vitro evolution of H5N1 avian influenza virus toward human-type receptor specificity
Identifieur interne : 000783 ( Pmc/Corpus ); précédent : 000782; suivant : 000784In vitro evolution of H5N1 avian influenza virus toward human-type receptor specificity
Auteurs : Li-Mei Chen ; Ola Blixt ; James Stevens ; Aleksandr S. Lipatov ; Charles T. Davis ; Brian E. Collins ; Nancy J. Cox ; James C. Paulson ; Ruben O. DonisSource :
- Virology [ 0042-6822 ] ; 2011.
Abstract
Acquisition of α2-6 sialoside receptor specificity by α2-3 specific highly-pathogenic avian influenza viruses (H5N1) is thought to be a prerequisite for efficient transmission in humans. By in vitro selection for binding α2-6 sialosides, we identified four variant viruses with amino acid substitutions in the hemagglutinin (S227N, D187G, E190G, and Q196R) that revealed modestly increased α2-6 and minimally decreased α2-3 binding by glycan array analysis. However, a mutant virus combining Q196R with mutations from previous pandemic viruses (Q226L and G228S) revealed predominantly α2-6 binding. Unlike the wild type H5N1, this mutant virus was transmitted by direct contact in the ferret model although not by airborne respiratory droplets. However, a reassortant virus with the mutant hemagglutinin, a human N2 neuraminidase and internal genes from an H5N1 virus was partially transmitted via respiratory droplets. The complex changes required for airborne transmissibility in ferrets suggest that extensive evolution is needed for H5N1 transmissibility in humans.
Url:
DOI: 10.1016/j.virol.2011.10.006
PubMed: 22056389
PubMed Central: 5480292
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PMC:5480292Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en"><italic>In vitro</italic> evolution of H5N1 avian influenza virus toward human-type receptor specificity</title><author><name sortKey="Chen, Li Mei" sort="Chen, Li Mei" uniqKey="Chen L" first="Li-Mei" last="Chen">Li-Mei Chen</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Blixt, Ola" sort="Blixt, Ola" uniqKey="Blixt O" first="Ola" last="Blixt">Ola Blixt</name><affiliation><nlm:aff id="A2">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Stevens, James" sort="Stevens, James" uniqKey="Stevens J" first="James" last="Stevens">James Stevens</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A3">Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Lipatov, Aleksandr S" sort="Lipatov, Aleksandr S" uniqKey="Lipatov A" first="Aleksandr S." last="Lipatov">Aleksandr S. Lipatov</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Davis, Charles T" sort="Davis, Charles T" uniqKey="Davis C" first="Charles T." last="Davis">Charles T. Davis</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Collins, Brian E" sort="Collins, Brian E" uniqKey="Collins B" first="Brian E." last="Collins">Brian E. Collins</name><affiliation><nlm:aff id="A2">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Cox, Nancy J" sort="Cox, Nancy J" uniqKey="Cox N" first="Nancy J." last="Cox">Nancy J. Cox</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><affiliation><nlm:aff id="A2">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Donis, Ruben O" sort="Donis, Ruben O" uniqKey="Donis R" first="Ruben O." last="Donis">Ruben O. Donis</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22056389</idno><idno type="pmc">5480292</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5480292</idno><idno type="RBID">PMC:5480292</idno><idno type="doi">10.1016/j.virol.2011.10.006</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000783</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000783</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main"><italic>In vitro</italic> evolution of H5N1 avian influenza virus toward human-type receptor specificity</title><author><name sortKey="Chen, Li Mei" sort="Chen, Li Mei" uniqKey="Chen L" first="Li-Mei" last="Chen">Li-Mei Chen</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Blixt, Ola" sort="Blixt, Ola" uniqKey="Blixt O" first="Ola" last="Blixt">Ola Blixt</name><affiliation><nlm:aff id="A2">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Stevens, James" sort="Stevens, James" uniqKey="Stevens J" first="James" last="Stevens">James Stevens</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A3">Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Lipatov, Aleksandr S" sort="Lipatov, Aleksandr S" uniqKey="Lipatov A" first="Aleksandr S." last="Lipatov">Aleksandr S. Lipatov</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Davis, Charles T" sort="Davis, Charles T" uniqKey="Davis C" first="Charles T." last="Davis">Charles T. Davis</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Collins, Brian E" sort="Collins, Brian E" uniqKey="Collins B" first="Brian E." last="Collins">Brian E. Collins</name><affiliation><nlm:aff id="A2">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Cox, Nancy J" sort="Cox, Nancy J" uniqKey="Cox N" first="Nancy J." last="Cox">Nancy J. Cox</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author><author><name sortKey="Paulson, James C" sort="Paulson, James C" uniqKey="Paulson J" first="James C." last="Paulson">James C. Paulson</name><affiliation><nlm:aff id="A2">Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation><affiliation><nlm:aff id="A4">Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</nlm:aff></affiliation></author><author><name sortKey="Donis, Ruben O" sort="Donis, Ruben O" uniqKey="Donis R" first="Ruben O." last="Donis">Ruben O. Donis</name><affiliation><nlm:aff id="A1">Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</nlm:aff></affiliation></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2011">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p id="P1">Acquisition of α2-6 sialoside receptor specificity by α2-3 specific highly-pathogenic avian influenza viruses (H5N1) is thought to be a prerequisite for efficient transmission in humans. By in vitro selection for binding α2-6 sialosides, we identified four variant viruses with amino acid substitutions in the hemagglutinin (S227N, D187G, E190G, and Q196R) that revealed modestly increased α2-6 and minimally decreased α2-3 binding by glycan array analysis. However, a mutant virus combining Q196R with mutations from previous pandemic viruses (Q226L and G228S) revealed predominantly α2-6 binding. Unlike the wild type H5N1, this mutant virus was transmitted by direct contact in the ferret model although not by airborne respiratory droplets. However, a reassortant virus with the mutant hemagglutinin, a human N2 neuraminidase and internal genes from an H5N1 virus was partially transmitted via respiratory droplets. The complex changes required for airborne transmissibility in ferrets suggest that extensive evolution is needed for H5N1 transmissibility in humans.</p></div></front></TEI><pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<pmc-dir>properties manuscript</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-journal-id">0110674</journal-id><journal-id journal-id-type="pubmed-jr-id">8015</journal-id><journal-id journal-id-type="nlm-ta">Virology</journal-id><journal-id journal-id-type="iso-abbrev">Virology</journal-id><journal-title-group><journal-title>Virology</journal-title></journal-title-group><issn pub-type="ppub">0042-6822</issn><issn pub-type="epub">1096-0341</issn></journal-meta><article-meta><article-id pub-id-type="pmid">22056389</article-id><article-id pub-id-type="pmc">5480292</article-id><article-id pub-id-type="doi">10.1016/j.virol.2011.10.006</article-id><article-id pub-id-type="manuscript">NIHMS864684</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title><italic>In vitro</italic> evolution of H5N1 avian influenza virus toward human-type receptor specificity</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Chen</surname><given-names>Li-Mei</given-names></name><xref ref-type="aff" rid="A1">a</xref><xref rid="FN2" ref-type="author-notes">1</xref></contrib><contrib contrib-type="author"><name><surname>Blixt</surname><given-names>Ola</given-names></name><xref ref-type="aff" rid="A2">b</xref><xref ref-type="aff" rid="A4">d</xref><xref rid="FN2" ref-type="author-notes">1</xref><xref rid="FN3" ref-type="author-notes">2</xref></contrib><contrib contrib-type="author"><name><surname>Stevens</surname><given-names>James</given-names></name><xref ref-type="aff" rid="A1">a</xref><xref ref-type="aff" rid="A3">c</xref></contrib><contrib contrib-type="author"><name><surname>Lipatov</surname><given-names>Aleksandr S.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Davis</surname><given-names>Charles T.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Collins</surname><given-names>Brian E.</given-names></name><xref ref-type="aff" rid="A2">b</xref><xref ref-type="aff" rid="A4">d</xref></contrib><contrib contrib-type="author"><name><surname>Cox</surname><given-names>Nancy J.</given-names></name><xref ref-type="aff" rid="A1">a</xref></contrib><contrib contrib-type="author"><name><surname>Paulson</surname><given-names>James C.</given-names></name><xref ref-type="aff" rid="A2">b</xref><xref ref-type="aff" rid="A4">d</xref><xref rid="FN2" ref-type="author-notes">1</xref></contrib><contrib contrib-type="author"><name><surname>Donis</surname><given-names>Ruben O.</given-names></name><xref ref-type="aff" rid="A1">a</xref><xref rid="FN1" ref-type="author-notes">*</xref><xref rid="FN2" ref-type="author-notes">1</xref></contrib></contrib-group><aff id="A1"><label>a</label>Influenza Division, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States</aff><aff id="A2"><label>b</label>Department of Chemical Physiology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</aff><aff id="A3"><label>c</label>Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</aff><aff id="A4"><label>d</label>Glycan Array Synthesis Core-D, Consortium for Functional Glycomics, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, United States</aff><author-notes><corresp id="FN1"><label>*</label>Corresponding author at: Influenza Division, Mailstop G-16, Centers for Disease Control and Prevention, 1600 Clifton Road, Atlanta, GA 30333, United States. Fax: +1 404 639 2350. <email>rdonis@cdc.gov</email> (R.O. Donis)</corresp><fn id="FN2" fn-type="equal"><label>1</label><p>Denotes equal contribution.</p></fn><fn id="FN3" fn-type="present-address"><label>2</label><p>Current address: Department of Cellular and Molecular Medicine, University of Copenhagen, Copenhagen DK-2200N, Denmark.</p></fn></author-notes><pub-date pub-type="nihms-submitted"><day>17</day><month>4</month><year>2017</year></pub-date><pub-date pub-type="epub"><day>05</day><month>11</month><year>2011</year></pub-date><pub-date pub-type="ppub"><day>05</day><month>1</month><year>2012</year></pub-date><pub-date pub-type="pmc-release"><day>22</day><month>6</month><year>2017</year></pub-date><volume>422</volume><issue>1</issue><fpage>105</fpage><lpage>113</lpage><pmc-comment>elocation-id from pubmed: 10.1016/j.virol.2011.10.006</pmc-comment>
<abstract><p id="P1">Acquisition of α2-6 sialoside receptor specificity by α2-3 specific highly-pathogenic avian influenza viruses (H5N1) is thought to be a prerequisite for efficient transmission in humans. By in vitro selection for binding α2-6 sialosides, we identified four variant viruses with amino acid substitutions in the hemagglutinin (S227N, D187G, E190G, and Q196R) that revealed modestly increased α2-6 and minimally decreased α2-3 binding by glycan array analysis. However, a mutant virus combining Q196R with mutations from previous pandemic viruses (Q226L and G228S) revealed predominantly α2-6 binding. Unlike the wild type H5N1, this mutant virus was transmitted by direct contact in the ferret model although not by airborne respiratory droplets. However, a reassortant virus with the mutant hemagglutinin, a human N2 neuraminidase and internal genes from an H5N1 virus was partially transmitted via respiratory droplets. The complex changes required for airborne transmissibility in ferrets suggest that extensive evolution is needed for H5N1 transmissibility in humans.</p></abstract><kwd-group><kwd>Highly pathogenic avian influenza virus</kwd><kwd>Hemagglutinin</kwd><kwd>Host cell receptor</kwd><kwd>Virus attachment</kwd><kwd>H5N1</kwd><kwd>Sialoglycan</kwd><kwd>Host range</kwd><kwd>Pandemic virus emergence</kwd></kwd-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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