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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin
<xref ref-type="fn" rid="FN2"><sup>▿</sup></xref><xref ref-type="fn" rid="FN1">†</xref></title><author><name sortKey="Xu, Rui" sort="Xu, Rui" uniqKey="Xu R" first="Rui" last="Xu">Rui Xu</name><affiliation><nlm:aff id="aff1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</nlm:aff></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation><nlm:aff id="aff1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">21367895</idno><idno type="pmc">3126156</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3126156</idno><idno type="RBID">PMC:3126156</idno><idno type="doi">10.1128/JVI.02430-10</idno><date when="2011">2011</date><idno type="wicri:Area/Pmc/Corpus">000634</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000634</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin
<xref ref-type="fn" rid="FN2"><sup>▿</sup></xref><xref ref-type="fn" rid="FN1">†</xref></title><author><name sortKey="Xu, Rui" sort="Xu, Rui" uniqKey="Xu R" first="Rui" last="Xu">Rui Xu</name><affiliation><nlm:aff id="aff1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</nlm:aff></affiliation></author><author><name sortKey="Wilson, Ian A" sort="Wilson, Ian A" uniqKey="Wilson I" first="Ian A." last="Wilson">Ian A. Wilson</name><affiliation><nlm:aff id="aff1">Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</nlm:aff></affiliation><affiliation><nlm:aff id="aff2">Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</nlm:aff></affiliation></author></analytic><series><title level="j">Journal of Virology</title><idno type="ISSN">0022-538X</idno><idno type="eISSN">1098-5514</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>The hemagglutinin (HA) envelope protein of influenza virus mediates viral entry through membrane fusion in the acidic environment of the endosome. Crystal structures of HA in pre- and postfusion states have laid the foundation for proposals for a general fusion mechanism for viral envelope proteins. The large-scale conformational rearrangement of HA at low pH is triggered by a loop-to-helix transition of an interhelical loop (B loop) within the fusion domain and is often referred to as the “spring-loaded” mechanism. Although the receptor-binding HA1 subunit is believed to act as a “clamp” to keep the B loop in its metastable prefusion state at neutral pH, the “pH sensors” that are responsible for the clamp release and the ensuing structural transitions have remained elusive. Here we identify a mutation in the HA2 fusion domain from the influenza virus H2 subtype that stabilizes the HA trimer in a prefusion-like state at and below fusogenic pH. Crystal structures of this putative early intermediate state reveal reorganization of ionic interactions at the HA1-HA2 interface at acidic pH and deformation of the HA1 membrane-distal domain. Along with neutralization of glutamate residues on the B loop, these changes cause a rotation of the B loop and solvent exposure of conserved phenylalanines, which are key residues at the trimer interface of the postfusion structure. Thus, our study reveals the possible initial structural event that leads to release of the B loop from its prefusion conformation, which is aided by unexpected structural changes within the membrane-distal HA1 domain at low pH.</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>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Virol</journal-id><journal-id journal-id-type="hwp">jvi</journal-id><journal-id journal-id-type="pmc">jvi</journal-id><journal-id journal-id-type="publisher-id">JVI</journal-id><journal-title-group><journal-title>Journal of Virology</journal-title></journal-title-group><issn pub-type="ppub">0022-538X</issn><issn pub-type="epub">1098-5514</issn><publisher><publisher-name>American Society for Microbiology</publisher-name><publisher-loc>1752 N St., N.W., Washington, DC</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21367895</article-id><article-id pub-id-type="pmc">3126156</article-id><article-id pub-id-type="publisher-id">2430-10</article-id><article-id pub-id-type="doi">10.1128/JVI.02430-10</article-id><article-categories><subj-group subj-group-type="heading"><subject>Structure and Assembly</subject></subj-group></article-categories><title-group><article-title>Structural Characterization of an Early Fusion Intermediate of Influenza Virus Hemagglutinin
<xref ref-type="fn" rid="FN2"><sup>▿</sup></xref><xref ref-type="fn" rid="FN1">†</xref></article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Xu</surname><given-names>Rui</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Wilson</surname><given-names>Ian A.</given-names></name><xref ref-type="aff" rid="aff1"><sup>1</sup></xref><xref ref-type="aff" rid="aff2"><sup>2</sup></xref><xref ref-type="corresp" rid="cor1">*</xref></contrib><aff id="aff1"><label>1</label>Department of Molecular Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</aff><aff id="aff2"><label>2</label>Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037</aff></contrib-group><author-notes><corresp id="cor1"><label>*</label>Corresponding author. Mailing address: <addr-line>Department of Molecular Biology, BCC-206, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037</addr-line>. Phone: <phone>(858) 784-9706</phone>. Fax: <fax>(858) 784-2980</fax>. E-mail: <email>wilson@scripps.edu</email>.</corresp></author-notes><pub-date pub-type="ppub"><month>5</month><year>2011</year></pub-date><volume>85</volume><issue>10</issue><fpage>5172</fpage><lpage>5182</lpage><history><date date-type="received"><day>21</day><month>11</month><year>2010</year></date><date date-type="accepted"><day>22</day><month>2</month><year>2011</year></date></history><permissions><copyright-statement>Copyright © 2011, American Society for Microbiology</copyright-statement><copyright-year>2011</copyright-year><copyright-holder>American Society for Microbiology</copyright-holder></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zjv01011005172.pdf"></self-uri><abstract><p>The hemagglutinin (HA) envelope protein of influenza virus mediates viral entry through membrane fusion in the acidic environment of the endosome. Crystal structures of HA in pre- and postfusion states have laid the foundation for proposals for a general fusion mechanism for viral envelope proteins. The large-scale conformational rearrangement of HA at low pH is triggered by a loop-to-helix transition of an interhelical loop (B loop) within the fusion domain and is often referred to as the “spring-loaded” mechanism. Although the receptor-binding HA1 subunit is believed to act as a “clamp” to keep the B loop in its metastable prefusion state at neutral pH, the “pH sensors” that are responsible for the clamp release and the ensuing structural transitions have remained elusive. Here we identify a mutation in the HA2 fusion domain from the influenza virus H2 subtype that stabilizes the HA trimer in a prefusion-like state at and below fusogenic pH. Crystal structures of this putative early intermediate state reveal reorganization of ionic interactions at the HA1-HA2 interface at acidic pH and deformation of the HA1 membrane-distal domain. Along with neutralization of glutamate residues on the B loop, these changes cause a rotation of the B loop and solvent exposure of conserved phenylalanines, which are key residues at the trimer interface of the postfusion structure. Thus, our study reveals the possible initial structural event that leads to release of the B loop from its prefusion conformation, which is aided by unexpected structural changes within the membrane-distal HA1 domain at low pH.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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