A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2
Identifieur interne : 000A95 ( Pmc/Checkpoint ); précédent : 000A94; suivant : 000A96A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2
Auteurs : Anna-Winona Struck [Allemagne] ; Marco Axmann [Allemagne] ; Susanne Pfefferle [Allemagne] ; Christian Drosten [Allemagne] ; Bernd Meyer [Allemagne]Source :
- Antiviral Research [ 0166-3542 ] ; 2012.
Abstract
► Hexapeptide YKYRYL specifically inhibits SARS infection in cells. ► Assessment of peptide libraries by SPR screening and virus proliferation assays. ► Hexapeptide YKYRYL is minimal binding epitope of SARS spike protein to ACE2. ► Characterization by SPR, STD and molecular dynamics of the binding mode of the hexapeptide.
Url:
DOI: 10.1016/j.antiviral.2011.12.012
PubMed: 22265858
PubMed Central: 7114193
Affiliations:
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sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement 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type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114193</idno><idno type="RBID">PMC:7114193</idno><idno type="doi">10.1016/j.antiviral.2011.12.012</idno><date when="2012">2012</date><idno type="wicri:Area/Pmc/Corpus">000D92</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">000D92</idno><idno type="wicri:Area/Pmc/Curation">000D92</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">000D92</idno><idno type="wicri:Area/Pmc/Checkpoint">000A95</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000A95</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2</title><author><name sortKey="Struck, Anna Winona" sort="Struck, Anna Winona" uniqKey="Struck A" first="Anna-Winona" last="Struck">Anna-Winona Struck</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><affiliation wicri:level="1"><nlm:aff id="aff2">Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg</wicri:regionArea><wicri:noRegion>20359 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author><author><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name><affiliation wicri:level="1"><nlm:aff id="aff1">Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</nlm:aff><country xml:lang="fr">Allemagne</country><wicri:regionArea>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg</wicri:regionArea><wicri:noRegion>20146 Hamburg</wicri:noRegion><placeName><settlement type="city">Hambourg</settlement><region type="land" nuts="2">Hambourg</region></placeName></affiliation></author></analytic><series><title level="j">Antiviral Research</title><idno type="ISSN">0166-3542</idno><idno type="eISSN">1872-9096</idno><imprint><date when="2012">2012</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><sec><title>Graphical abstract</title><p><fig id="f0040" position="anchor"><graphic xlink:href="fx1"></graphic></fig></p></sec><sec><title>Highlights</title><p>► Hexapeptide YKYRYL specifically inhibits SARS infection in cells. ► Assessment of peptide libraries by SPR screening and virus proliferation assays. ► Hexapeptide YKYRYL is minimal binding epitope of SARS spike protein to ACE2. ► Characterization by SPR, STD and molecular dynamics of the binding mode of the hexapeptide.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Babcock, G J" uniqKey="Babcock G">G.J. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Antiviral Res</journal-id><journal-id journal-id-type="iso-abbrev">Antiviral Res</journal-id><journal-title-group><journal-title>Antiviral Research</journal-title></journal-title-group><issn pub-type="ppub">0166-3542</issn><issn pub-type="epub">1872-9096</issn><publisher><publisher-name>Elsevier B.V.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">22265858</article-id><article-id pub-id-type="pmc">7114193</article-id><article-id pub-id-type="publisher-id">S0166-3542(11)00548-1</article-id><article-id pub-id-type="doi">10.1016/j.antiviral.2011.12.012</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>A hexapeptide of the receptor-binding domain of SARS corona virus spike protein blocks viral entry into host cells via the human receptor ACE2</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Struck</surname><given-names>Anna-Winona</given-names></name><xref rid="aff1" ref-type="aff">a</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Axmann</surname><given-names>Marco</given-names></name><xref rid="aff1" ref-type="aff">a</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Pfefferle</surname><given-names>Susanne</given-names></name><xref rid="aff2" ref-type="aff">b</xref><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author"><name><surname>Drosten</surname><given-names>Christian</given-names></name><email>drosten@virology-bonn.de</email><xref rid="aff2" ref-type="aff">b</xref><xref rid="cor1" ref-type="corresp">⁎</xref></contrib><contrib contrib-type="author"><name><surname>Meyer</surname><given-names>Bernd</given-names></name><email>Bernd.Meyer@chemie.uni-hamburg.de</email><xref rid="aff1" ref-type="aff">a</xref><xref rid="cor1" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="aff1"><label>a</label>Organic Chemistry, Department of Chemistry, Faculty of Sciences, University of Hamburg, Martin Luther King Place 6, 20146 Hamburg, Germany</aff><aff id="aff2"><label>b</label>Department of Virology, Bernhard Nocht Institute for Tropical Medicine, Bernhard-Nocht-Str. 74, 20359 Hamburg, Germany</aff><author-notes><corresp id="cor1"><label>⁎</label>Corresponding authors. Present address: University Hospital Bonn, Institute of Virology, Sigmund-Freud-Str.25, 53127 Bonn, Germany. Tel.: +49 228 287 11055 (C. Drosten), Tel.: +49 40 42838 5913 (B. Meyer). <email>drosten@virology-bonn.de</email><email>Bernd.Meyer@chemie.uni-hamburg.de</email></corresp><fn id="fn1"><label>1</label><p>These coauthors contributed equally to the paper.</p></fn></author-notes><pub-date pub-type="pmc-release"><day>16</day><month>1</month><year>2012</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><month>6</month><year>2012</year></pub-date><pub-date pub-type="epub"><day>16</day><month>1</month><year>2012</year></pub-date><volume>94</volume><issue>3</issue><fpage>288</fpage><lpage>296</lpage><history><date date-type="received"><day>14</day><month>9</month><year>2011</year></date><date date-type="rev-recd"><day>16</day><month>12</month><year>2011</year></date><date date-type="accepted"><day>20</day><month>12</month><year>2011</year></date></history><permissions><copyright-statement>Copyright © 2011 Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2011</copyright-year><copyright-holder>Elsevier B.V.</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract abstract-type="graphical"><sec><title>Graphical abstract</title><p><fig id="f0040" position="anchor"><graphic xlink:href="fx1"></graphic></fig></p></sec><sec><title>Highlights</title><p>► Hexapeptide YKYRYL specifically inhibits SARS infection in cells. ► Assessment of peptide libraries by SPR screening and virus proliferation assays. ► Hexapeptide YKYRYL is minimal binding epitope of SARS spike protein to ACE2. ► Characterization by SPR, STD and molecular dynamics of the binding mode of the hexapeptide.</p></sec></abstract><abstract><p><italic>In vitro</italic> infection of Vero E6 cells by SARS coronavirus (SARS-CoV) is blocked by hexapeptide Tyr-Lys-Tyr-Arg-Tyr-Leu. The peptide also inhibits proliferation of coronavirus NL63. On human cells both viruses utilize angiotensin-converting enzyme 2 (ACE2) as entry receptor. Blocking the viral entry is specific as alpha virus Sindbis shows no reduction in infectivity. Peptide <sup>438</sup>YKYRYL<sup>443</sup> is part of the receptor-binding domain (RBD) of the spike protein of SARS-CoV. Peptide libraries were screened by surface plasmon resonance (SPR) to identify RBD binding epitopes. <sup>438</sup>YKYRYL<sup>443</sup> carries the dominant binding epitope and binds to ACE2 with <italic>K</italic><sub>D</sub> = 46 μM. The binding mode was further characterized by saturation transfer difference (STD) NMR spectroscopy and molecular dynamic simulations. Based on this information the peptide can be used as lead structure to design potential entry inhibitors against SARS-CoV and related viruses.</p></abstract><kwd-group><title>Keywords</title><kwd>SARS coronavirus</kwd><kwd>Spike protein</kwd><kwd>ACE2</kwd><kwd>Entry inhibitor</kwd><kwd>Virus proliferation assay</kwd><kwd>SPR screening</kwd></kwd-group></article-meta></front></pmc><affiliations><list><country><li>Allemagne</li></country><region><li>Hambourg</li></region><settlement><li>Hambourg</li></settlement></list><tree><country name="Allemagne"><region name="Hambourg"><name sortKey="Struck, Anna Winona" sort="Struck, Anna Winona" uniqKey="Struck A" first="Anna-Winona" last="Struck">Anna-Winona Struck</name></region><name sortKey="Axmann, Marco" sort="Axmann, Marco" uniqKey="Axmann M" first="Marco" last="Axmann">Marco Axmann</name><name sortKey="Drosten, Christian" sort="Drosten, Christian" uniqKey="Drosten C" first="Christian" last="Drosten">Christian Drosten</name><name sortKey="Meyer, Bernd" sort="Meyer, Bernd" uniqKey="Meyer B" first="Bernd" last="Meyer">Bernd Meyer</name><name sortKey="Pfefferle, Susanne" sort="Pfefferle, Susanne" uniqKey="Pfefferle S" first="Susanne" last="Pfefferle">Susanne Pfefferle</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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