On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus
Identifieur interne : 000C04 ( Pmc/Checkpoint ); précédent : 000C03; suivant : 000C05On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus
Auteurs : Zai Wang ; Jian-Dong Huang ; Kin-Ling Wong ; Pei-Gang Wang ; Hao-Jie Zhang ; Julian A. Tanner ; Ottavia Spiga ; Andrea Bernini ; Bo-Jian Zheng ; Neri NiccolaiSource :
- The Febs Journal [ 1742-464X ] ; 2010.
Abstract
In a previous study, severe acute respiratory syndrome coronavirus (SARS‐CoV) was cultured in the presence of bananin, an effective adamantane‐related molecule with antiviral activity. In the present study, we show that all bananin‐resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS‐CoV bananin‐resistant variants was performed. The S259/L mutation of SARS‐CoV helicase is always found in all the identified bananin‐resistant variants, suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS‐CoV predicted helicase structure, S259 is found in a hydrophilic surface pocket, far from the enzyme active sites and outside the helicase dimer interface. The S/L substitution causes a pocket volume reduction that weakens the interaction between bananin and SARS‐CoV mutated helicase, suggesting a possible mechanism for bananin antiviral activity.
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DOI: 10.1111/j.1742-4658.2010.07961.x
PubMed: 21134131
PubMed Central: 7164005
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Tanner</name><affiliation><nlm:aff id="a1"></nlm:aff></affiliation></author><author><name sortKey="Spiga, Ottavia" sort="Spiga, Ottavia" uniqKey="Spiga O" first="Ottavia" last="Spiga">Ottavia Spiga</name><affiliation><nlm:aff id="a4"></nlm:aff></affiliation><affiliation><nlm:aff id="a5"></nlm:aff></affiliation></author><author><name sortKey="Bernini, Andrea" sort="Bernini, Andrea" uniqKey="Bernini A" first="Andrea" last="Bernini">Andrea Bernini</name><affiliation><nlm:aff id="a4"></nlm:aff></affiliation><affiliation><nlm:aff id="a5"></nlm:aff></affiliation></author><author><name sortKey="Zheng, Bo Ian" sort="Zheng, Bo Ian" uniqKey="Zheng B" first="Bo-Jian" last="Zheng">Bo-Jian Zheng</name><affiliation><nlm:aff id="a2"></nlm:aff></affiliation></author><author><name sortKey="Niccolai, Neri" sort="Niccolai, Neri" uniqKey="Niccolai N" first="Neri" last="Niccolai">Neri Niccolai</name><affiliation><nlm:aff id="a4"></nlm:aff></affiliation><affiliation><nlm:aff id="a5"></nlm:aff></affiliation></author></analytic><series><title level="j">The Febs Journal</title><idno type="ISSN">1742-464X</idno><idno type="eISSN">1742-4658</idno><imprint><date when="2010">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>In a previous study, severe acute respiratory syndrome coronavirus (SARS‐CoV) was cultured in the presence of bananin, an effective adamantane‐related molecule with antiviral activity. In the present study, we show that all bananin‐resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS‐CoV bananin‐resistant variants was performed. The S259/L mutation of SARS‐CoV helicase is always found in all the identified bananin‐resistant variants, suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS‐CoV predicted helicase structure, S259 is found in a hydrophilic surface pocket, far from the enzyme active sites and outside the helicase dimer interface. The S/L substitution causes a pocket volume reduction that weakens the interaction between bananin and SARS‐CoV mutated helicase, suggesting a possible mechanism for bananin antiviral activity.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct><analytic><author><name sortKey="Dayhoff, Mo" uniqKey="Dayhoff M">MO Dayhoff</name></author></analytic></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct><biblStruct></biblStruct></listBibl></div1></back></TEI><pmc article-type="research-article"><pmc-dir>properties open_access</pmc-dir>
<front><journal-meta><journal-id journal-id-type="nlm-ta">FEBS J</journal-id><journal-id journal-id-type="iso-abbrev">FEBS J</journal-id><journal-id journal-id-type="doi">10.1111/(ISSN)1742-4658</journal-id><journal-id journal-id-type="publisher-id">FEBS</journal-id><journal-title-group><journal-title>The Febs Journal</journal-title></journal-title-group><issn pub-type="ppub">1742-464X</issn><issn pub-type="epub">1742-4658</issn><publisher><publisher-name>Blackwell Publishing Ltd</publisher-name><publisher-loc>Oxford, UK</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">21134131</article-id><article-id pub-id-type="pmc">7164005</article-id><article-id pub-id-type="doi">10.1111/j.1742-4658.2010.07961.x</article-id><article-id pub-id-type="publisher-id">FEBS7961</article-id><article-categories><subj-group subj-group-type="heading"><subject>Original Articles</subject></subj-group></article-categories><title-group><article-title>On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus</article-title><alt-title alt-title-type="left-running-head">Z. Wang <italic>et al.</italic></alt-title><alt-title alt-title-type="right-running-head">Mechanisms of bananin activity against SARS‐CoV</alt-title></title-group><contrib-group><contrib id="cr1" contrib-type="author"><name><surname>Wang</surname><given-names>Zai</given-names></name><xref ref-type="aff" rid="a1"><sup>1</sup></xref></contrib><contrib id="cr2" contrib-type="author"><name><surname>Huang</surname><given-names>Jian‐Dong</given-names></name><xref ref-type="aff" rid="a1"><sup>1</sup></xref></contrib><contrib id="cr3" contrib-type="author"><name><surname>Wong</surname><given-names>Kin‐Ling</given-names></name><xref ref-type="aff" rid="a2"><sup>2</sup></xref></contrib><contrib id="cr4" contrib-type="author"><name><surname>Wang</surname><given-names>Pei‐Gang</given-names></name><xref ref-type="aff" rid="a3"><sup>3</sup></xref></contrib><contrib id="cr5" contrib-type="author"><name><surname>Zhang</surname><given-names>Hao‐Jie</given-names></name><xref ref-type="aff" rid="a2"><sup>2</sup></xref></contrib><contrib id="cr6" contrib-type="author"><name><surname>Tanner</surname><given-names>Julian A.</given-names></name><xref ref-type="aff" rid="a1"><sup>1</sup></xref></contrib><contrib id="cr7" contrib-type="author"><name><surname>Spiga</surname><given-names>Ottavia</given-names></name><xref ref-type="aff" rid="a4"><sup>4</sup></xref><xref ref-type="aff" rid="a5"><sup>5</sup></xref></contrib><contrib id="cr8" contrib-type="author"><name><surname>Bernini</surname><given-names>Andrea</given-names></name><xref ref-type="aff" rid="a4"><sup>4</sup></xref><xref ref-type="aff" rid="a5"><sup>5</sup></xref></contrib><contrib id="cr9" contrib-type="author"><name><surname>Zheng</surname><given-names>Bo‐Jian</given-names></name><xref ref-type="aff" rid="a2"><sup>2</sup></xref></contrib><contrib id="cr10" contrib-type="author"><name><surname>Niccolai</surname><given-names>Neri</given-names></name><xref ref-type="aff" rid="a4"><sup>4</sup></xref><xref ref-type="aff" rid="a5"><sup>5</sup></xref></contrib></contrib-group><aff id="a1"><label><sup>1</sup></label> Department of Biochemistry, Faculty of Medicine, University of Hong Kong, China</aff><aff id="a2"><label><sup>2</sup></label> Department of Microbiology, Faculty of Medicine, University of Hong Kong, China</aff><aff id="a3"><label><sup>3</sup></label> The HKU‐Pasteur Research Centre (HKU‐PRC), Pokfulam, Hong Kong SAR, China</aff><aff id="a4"><label><sup>4</sup></label> Department of Molecular Biology, University of Siena, Italy</aff><aff id="a5"><label><sup>5</sup></label> SienaBiografix Srl, Siena, Italy</aff><author-notes><corresp id="correspondenceTo">J.‐D. Huang or N. Niccolai, Department of Biochemistry, University of Hong Kong, 3/F Laboratory Block, Faculty of Medicine Building, 21 Sassoon Road, Pokfulam, Hong Kong SAR, China; Department of Molecular Biology, University of Siena, I‐53100 Siena, Italy
Fax: +852 2855 1254; +39 0577 234903
Tel: +852 2819 2810; +39 0577 234910
E‐mail: <email>jdhuang@hkucc.hku.hk</email>; <email>niccolai@unisi.it</email></corresp></author-notes><pub-date pub-type="ppub"><month>1</month><year>2011</year></pub-date><pub-date pub-type="epub"><day>06</day><month>12</month><year>2010</year></pub-date><volume>278</volume><issue>2</issue><issue-id pub-id-type="doi">10.1111/ejb.2010.278.issue-2</issue-id><fpage>383</fpage><lpage>389</lpage><history><pmc-comment>supplied string: (Received 28 June 2010, revised 9 November 2010, accepted 12 November 2010)</pmc-comment>
<date date-type="received"><day>28</day><month>6</month><year>2010</year></date><date date-type="rev-recd"><day>9</day><month>11</month><year>2010</year></date><date date-type="accepted"><day>12</day><month>11</month><year>2010</year></date></history><permissions><copyright-statement content-type="article-copyright">© 2010 The Authors Journal compilation © 2010 FEBS</copyright-statement><license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="file:FEBS-278-383.pdf"></self-uri><abstract><p>In a previous study, severe acute respiratory syndrome coronavirus (SARS‐CoV) was cultured in the presence of bananin, an effective adamantane‐related molecule with antiviral activity. In the present study, we show that all bananin‐resistant variants exhibit mutations in helicase and membrane protein, although no evidence of bananin interference on their mutual interaction has been found. A structural analysis on protein sequence mutations found in SARS‐CoV bananin‐resistant variants was performed. The S259/L mutation of SARS‐CoV helicase is always found in all the identified bananin‐resistant variants, suggesting a primary role of this mutation site for bananin activity. From a structural analysis of SARS‐CoV predicted helicase structure, S259 is found in a hydrophilic surface pocket, far from the enzyme active sites and outside the helicase dimer interface. The S/L substitution causes a pocket volume reduction that weakens the interaction between bananin and SARS‐CoV mutated helicase, suggesting a possible mechanism for bananin antiviral activity.</p></abstract><kwd-group><kwd id="k1">antiviral drugs</kwd><kwd id="k2">bananin</kwd><kwd id="k3">coronavirus</kwd><kwd id="k4">viral helicase</kwd></kwd-group><counts><fig-count count="4"></fig-count><table-count count="1"></table-count><page-count count="7"></page-count></counts><custom-meta-group><custom-meta><meta-name>source-schema-version-number</meta-name><meta-value>2.0</meta-value></custom-meta><custom-meta><meta-name>cover-date</meta-name><meta-value>January 2011</meta-value></custom-meta><custom-meta><meta-name>details-of-publishers-convertor</meta-name><meta-value>Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Bernini, Andrea" sort="Bernini, Andrea" uniqKey="Bernini A" first="Andrea" last="Bernini">Andrea Bernini</name><name sortKey="Huang, Jian Ong" sort="Huang, Jian Ong" uniqKey="Huang J" first="Jian-Dong" last="Huang">Jian-Dong Huang</name><name sortKey="Niccolai, Neri" sort="Niccolai, Neri" uniqKey="Niccolai N" first="Neri" last="Niccolai">Neri Niccolai</name><name sortKey="Spiga, Ottavia" sort="Spiga, Ottavia" uniqKey="Spiga O" first="Ottavia" last="Spiga">Ottavia Spiga</name><name sortKey="Tanner, Julian A" sort="Tanner, Julian A" uniqKey="Tanner J" first="Julian A." last="Tanner">Julian A. Tanner</name><name sortKey="Wang, Pei Ang" sort="Wang, Pei Ang" uniqKey="Wang P" first="Pei-Gang" last="Wang">Pei-Gang Wang</name><name sortKey="Wang, Zai" sort="Wang, Zai" uniqKey="Wang Z" first="Zai" last="Wang">Zai Wang</name><name sortKey="Wong, Kin Ing" sort="Wong, Kin Ing" uniqKey="Wong K" first="Kin-Ling" last="Wong">Kin-Ling Wong</name><name sortKey="Zhang, Hao Ie" sort="Zhang, Hao Ie" uniqKey="Zhang H" first="Hao-Jie" last="Zhang">Hao-Jie Zhang</name><name sortKey="Zheng, Bo Ian" sort="Zheng, Bo Ian" uniqKey="Zheng B" first="Bo-Jian" last="Zheng">Bo-Jian Zheng</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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