Mechanisms of Host Receptor Adaptation by Severe Acute Respiratory Syndrome Coronavirus*
Identifieur interne : 001111 ( Pmc/Curation ); précédent : 001110; suivant : 001112Mechanisms of Host Receptor Adaptation by Severe Acute Respiratory Syndrome Coronavirus*
Auteurs : Kailang Wu ; Guiqing Peng ; Matthew Wilken ; Robert J. Geraghty [États-Unis] ; Fang LiSource :
- The Journal of Biological Chemistry [ 0021-9258 ] ; 2012.
Abstract
Url:
DOI: 10.1074/jbc.M111.325803
PubMed: 22291007
PubMed Central: 3308800
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Mechanisms of Host Receptor Adaptation by Severe Acute Respiratory
Syndrome Coronavirus<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Wu, Kailang" sort="Wu, Kailang" uniqKey="Wu K" first="Kailang" last="Wu">Kailang Wu</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wilken, Matthew" sort="Wilken, Matthew" uniqKey="Wilken M" first="Matthew" last="Wilken">Matthew Wilken</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Geraghty, Robert J" sort="Geraghty, Robert J" uniqKey="Geraghty R" first="Robert J." last="Geraghty">Robert J. Geraghty</name><affiliation wicri:level="2"><nlm:aff id="aff2">Center for Drug Design, University of Minnesota Medical School, Minneapolis, Minnesota 55455</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Minnesota</region></placeName><wicri:cityArea>Center for Drug Design, University of Minnesota Medical School, Minneapolis</wicri:cityArea></affiliation></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">22291007</idno><idno type="pmc">3308800</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3308800</idno><idno type="RBID">PMC:3308800</idno><idno type="doi">10.1074/jbc.M111.325803</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">001111</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001111</idno><idno type="wicri:Area/Pmc/Curation">001111</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001111</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Mechanisms of Host Receptor Adaptation by Severe Acute Respiratory
Syndrome Coronavirus<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></title><author><name sortKey="Wu, Kailang" sort="Wu, Kailang" uniqKey="Wu K" first="Kailang" last="Wu">Kailang Wu</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Peng, Guiqing" sort="Peng, Guiqing" uniqKey="Peng G" first="Guiqing" last="Peng">Guiqing Peng</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Wilken, Matthew" sort="Wilken, Matthew" uniqKey="Wilken M" first="Matthew" last="Wilken">Matthew Wilken</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author><author><name sortKey="Geraghty, Robert J" sort="Geraghty, Robert J" uniqKey="Geraghty R" first="Robert J." last="Geraghty">Robert J. Geraghty</name><affiliation wicri:level="2"><nlm:aff id="aff2">Center for Drug Design, University of Minnesota Medical School, Minneapolis, Minnesota 55455</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Minnesota</region></placeName><wicri:cityArea>Center for Drug Design, University of Minnesota Medical School, Minneapolis</wicri:cityArea></affiliation></author><author><name sortKey="Li, Fang" sort="Li, Fang" uniqKey="Li F" first="Fang" last="Li">Fang Li</name><affiliation><nlm:aff id="aff1"></nlm:aff></affiliation></author></analytic><series><title level="j">The Journal of Biological Chemistry</title><idno type="ISSN">0021-9258</idno><idno type="eISSN">1083-351X</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><bold>Background:</bold> The severe acute respiratory syndrome (SARS) virus has
undergone mutations in its receptor-binding domain.</p><p><bold>Results:</bold> We used biochemical, functional, and crystallographic
methods to investigate these mutations.</p><p><bold>Conclusion:</bold> These mutations were viral adaptations to either the
human or palm civet receptor.</p><p><bold>Significance:</bold> This research elucidates detailed mechanisms of host
receptor adaptation by the SARS virus and can help predict and monitor future
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<front><journal-meta><journal-id journal-id-type="nlm-ta">J Biol Chem</journal-id><journal-id journal-id-type="iso-abbrev">J. Biol. Chem</journal-id><journal-id journal-id-type="publisher-id">J. Biol. Chem</journal-id><journal-id journal-id-type="hwp">jbc</journal-id><journal-id journal-id-type="pmc">jbc</journal-id><journal-id journal-id-type="publisher-id">JBC</journal-id><journal-title-group><journal-title>The Journal of Biological Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0021-9258</issn><issn pub-type="epub">1083-351X</issn><publisher><publisher-name>American Society for Biochemistry and Molecular
Biology</publisher-name><publisher-loc>9650 Rockville Pike, Bethesda, MD 20814, U.S.A.</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22291007</article-id><article-id pub-id-type="pmc">3308800</article-id><article-id pub-id-type="publisher-id">M111.325803</article-id><article-id pub-id-type="doi">10.1074/jbc.M111.325803</article-id><article-categories><subj-group subj-group-type="heading"><subject>Microbiology</subject></subj-group></article-categories><title-group><article-title>Mechanisms of Host Receptor Adaptation by Severe Acute Respiratory
Syndrome Coronavirus<xref ref-type="fn" rid="FN1">*</xref><xref ref-type="fn" rid="FN2"><sup><inline-graphic xlink:href="sbox.jpg"></inline-graphic></sup></xref></article-title><alt-title alt-title-type="short">Evolution and Receptor Recognition of SARS
Virus</alt-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Wu</surname><given-names>Kailang</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Peng</surname><given-names>Guiqing</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Wilken</surname><given-names>Matthew</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="author-notes" rid="FN3"><sup>1</sup></xref></contrib><contrib contrib-type="author"><name><surname>Geraghty</surname><given-names>Robert J.</given-names></name><xref ref-type="aff" rid="aff2"><sup>§</sup></xref></contrib><contrib contrib-type="author"><name><surname>Li</surname><given-names>Fang</given-names></name><xref ref-type="aff" rid="aff1"><sup>‡</sup></xref><xref ref-type="corresp" rid="cor1"><sup>2</sup></xref></contrib><aff id="aff1">From the<label>‡</label>Department of Pharmacology and</aff><aff id="aff2"><label>§</label>Center for Drug Design, University of Minnesota Medical School, Minneapolis, Minnesota 55455</aff></contrib-group><author-notes><corresp id="cor1"><label>2</label> To whom correspondence should be addressed:
<addr-line>Dept. of Pharmacology, University of Minnesota Medical School,
6-121 Jackson Hall, 321 Church St. SE, Minneapolis, MN 55455.</addr-line>Tel.: <phone>612-625-6149</phone>; Fax: <fax>612-625-8408</fax>; E-mail:
<email>lifang@umn.edu</email>.</corresp><fn fn-type="equal" id="FN3"><label>1</label><p>These authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="ppub"><day>16</day><month>3</month><year>2012</year></pub-date><pub-date pub-type="epub"><day>30</day><month>1</month><year>2012</year></pub-date><volume>287</volume><issue>12</issue><fpage>8904</fpage><lpage>8911</lpage><history><date date-type="received"><day>21</day><month>11</month><year>2011</year></date><date date-type="rev-recd"><day>26</day><month>1</month><year>2012</year></date></history><permissions><copyright-statement>© 2012 by The American Society for Biochemistry and
Molecular Biology, Inc.</copyright-statement><copyright-year>2012</copyright-year><license><license-p>This article is made available via the PMC Open Access Subset for
unrestricted re-use and analyses in any form or by any means with
acknowledgement of the original source. These permissions are granted for
the duration of the COVID-19 pandemic or until permissions are revoked in
writing. Upon expiration of these permissions, PMC is granted a perpetual
license to make this article available via PMC and Europe PMC, consistent
with existing copyright protections.</license-p></license></permissions><self-uri xlink:title="pdf" xlink:type="simple" xlink:href="zbc01212008904.pdf"></self-uri><abstract abstract-type="teaser"><p><bold>Background:</bold> The severe acute respiratory syndrome (SARS) virus has
undergone mutations in its receptor-binding domain.</p><p><bold>Results:</bold> We used biochemical, functional, and crystallographic
methods to investigate these mutations.</p><p><bold>Conclusion:</bold> These mutations were viral adaptations to either the
human or palm civet receptor.</p><p><bold>Significance:</bold> This research elucidates detailed mechanisms of host
receptor adaptation by the SARS virus and can help predict and monitor future
evolution of the SARS virus in animals.</p></abstract><abstract><p>The severe acute respiratory syndrome coronavirus (SARS-CoV) from palm civets has
twice evolved the capacity to infect humans by gaining binding affinity for
human receptor angiotensin-converting enzyme 2 (ACE2). Numerous mutations have
been identified in the receptor-binding domain (RBD) of different SARS-CoV
strains isolated from humans or civets. Why these mutations were naturally
selected or how SARS-CoV evolved to adapt to different host receptors has been
poorly understood, presenting evolutionary and epidemic conundrums. In this
study, we investigated the impact of these mutations on receptor recognition, an
important determinant of SARS-CoV infection and pathogenesis. Using a
combination of biochemical, functional, and crystallographic approaches, we
elucidated the molecular and structural mechanisms of each of these naturally
selected RBD mutations. These mutations either strengthen favorable interactions
or reduce unfavorable interactions with two virus-binding hot spots on ACE2, and
by doing so, they enhance viral interactions with either human (hACE2) or civet
(cACE2) ACE2. Therefore, these mutations were viral adaptations to either hACE2
or cACE2. To corroborate the above analysis, we designed and characterized two
optimized RBDs. The human-optimized RBD contains all of the hACE2-adapted
residues (Phe-442, Phe-472, Asn-479, Asp-480, and Thr-487) and possesses
exceptionally high affinity for hACE2 but relative low affinity for cACE2. The
civet-optimized RBD contains all of the cACE2-adapted residues (Tyr-442,
Pro-472, Arg-479, Gly-480, and Thr-487) and possesses exceptionally high
affinity for cACE2 and also substantial affinity for hACE2. These results not
only illustrate the detailed mechanisms of host receptor adaptation by SARS-CoV
but also provide a molecular and structural basis for tracking future SARS-CoV
evolution in animals.</p></abstract><kwd-group><kwd>Crystallography</kwd><kwd>Evolution</kwd><kwd>Infectious Diseases</kwd><kwd>Receptors</kwd><kwd>Virus</kwd></kwd-group><funding-group><award-group><funding-source id="CS100">National Institutes of Health</funding-source><award-id rid="CS100">R01 AI089728</award-id></award-group></funding-group></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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