File Download
 
Links for fulltext
(May Require Subscription)
 
Supplementary

Article: On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus
  • Basic View
  • Metadata View
  • XML View
TitleOn the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus
 
AuthorsWang, Z1
Huang, JD1
Wong, KL1
Wang, PG3
Zhang, HJ1
Tanner, JA1
Spiga, O4 2
Bernini, A4 2
Zheng, BJ1
Niccolai, N4 2
 
Keywordsantiviral drugs
bananin
coronavirus
viral helicase
 
Issue Date2011
 
PublisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/
 
CitationFebs Journal, 2011, v. 278 n. 2, p. 383-389 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1742-4658.2010.07961.x
 
AbstractIn 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. © 2010 FEBS.
 
ISSN1742-464X
2012 Impact Factor: 4.25
2012 SCImago Journal Rankings: 1.658
 
DOIhttp://dx.doi.org/10.1111/j.1742-4658.2010.07961.x
 
ISI Accession Number IDWOS:000285877700018
Funding AgencyGrant Number
Research Fund for the Control of Infectious Diseases (RFCID)01030182
02040192
University of Siena
Funding Information:

Bananin was kindly provided by Dr A. J. Kesel (Chammunsterstrasse 47, D81827 Munchen, Germany). This work was supported by grants (01030182 and 02040192) from the Research Fund for the Control of Infectious Diseases (RFCID) awarded to Dr J. D. Huang and by grants from the University of Siena.

 
ReferencesReferences in Scopus
 
GrantsHelicases as antiviral drug targets
Determine the functions of the putative metal-binding domain of SARS-CoV helicase
 
DC FieldValue
dc.contributor.authorWang, Z
 
dc.contributor.authorHuang, JD
 
dc.contributor.authorWong, KL
 
dc.contributor.authorWang, PG
 
dc.contributor.authorZhang, HJ
 
dc.contributor.authorTanner, JA
 
dc.contributor.authorSpiga, O
 
dc.contributor.authorBernini, A
 
dc.contributor.authorZheng, BJ
 
dc.contributor.authorNiccolai, N
 
dc.date.accessioned2011-05-24T02:11:17Z
 
dc.date.available2011-05-24T02:11:17Z
 
dc.date.issued2011
 
dc.description.abstractIn 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. © 2010 FEBS.
 
dc.description.natureLink_to_subscribed_fulltext
 
dc.identifier.citationFebs Journal, 2011, v. 278 n. 2, p. 383-389 [How to Cite?]
DOI: http://dx.doi.org/10.1111/j.1742-4658.2010.07961.x
 
dc.identifier.citeulike8627024
 
dc.identifier.doihttp://dx.doi.org/10.1111/j.1742-4658.2010.07961.x
 
dc.identifier.epage389
 
dc.identifier.hkuros185117
 
dc.identifier.isiWOS:000285877700018
Funding AgencyGrant Number
Research Fund for the Control of Infectious Diseases (RFCID)01030182
02040192
University of Siena
Funding Information:

Bananin was kindly provided by Dr A. J. Kesel (Chammunsterstrasse 47, D81827 Munchen, Germany). This work was supported by grants (01030182 and 02040192) from the Research Fund for the Control of Infectious Diseases (RFCID) awarded to Dr J. D. Huang and by grants from the University of Siena.

 
dc.identifier.issn1742-464X
2012 Impact Factor: 4.25
2012 SCImago Journal Rankings: 1.658
 
dc.identifier.issue2
 
dc.identifier.openurl
 
dc.identifier.pmid21134131
 
dc.identifier.scopuseid_2-s2.0-78651078154
 
dc.identifier.spage383
 
dc.identifier.urihttp://hdl.handle.net/10722/133580
 
dc.identifier.volume278
 
dc.languageeng
 
dc.publisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/
 
dc.publisher.placeUnited Kingdom
 
dc.relation.ispartofFEBS Journal
 
dc.relation.projectHelicases as antiviral drug targets
 
dc.relation.projectDetermine the functions of the putative metal-binding domain of SARS-CoV helicase
 
dc.relation.referencesReferences in Scopus
 
dc.rightsThe definitive version is available at www.blackwell-synergy.com
 
dc.subjectantiviral drugs
 
dc.subjectbananin
 
dc.subjectcoronavirus
 
dc.subjectviral helicase
 
dc.titleOn the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus
 
dc.typeArticle
 
<?xml encoding="utf-8" version="1.0"?>
<item><contributor.author>Wang, Z</contributor.author>
<contributor.author>Huang, JD</contributor.author>
<contributor.author>Wong, KL</contributor.author>
<contributor.author>Wang, PG</contributor.author>
<contributor.author>Zhang, HJ</contributor.author>
<contributor.author>Tanner, JA</contributor.author>
<contributor.author>Spiga, O</contributor.author>
<contributor.author>Bernini, A</contributor.author>
<contributor.author>Zheng, BJ</contributor.author>
<contributor.author>Niccolai, N</contributor.author>
<date.accessioned>2011-05-24T02:11:17Z</date.accessioned>
<date.available>2011-05-24T02:11:17Z</date.available>
<date.issued>2011</date.issued>
<identifier.citation>Febs Journal, 2011, v. 278 n. 2, p. 383-389</identifier.citation>
<identifier.issn>1742-464X</identifier.issn>
<identifier.uri>http://hdl.handle.net/10722/133580</identifier.uri>
<description.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. &#169; 2010 FEBS.</description.abstract>
<language>eng</language>
<publisher>Wiley-Blackwell Publishing Ltd.. The Journal&apos;s web site is located at http://www.febsjournal.org/</publisher>
<relation.ispartof>FEBS Journal</relation.ispartof>
<rights>The definitive version is available at www.blackwell-synergy.com</rights>
<subject>antiviral drugs</subject>
<subject>bananin</subject>
<subject>coronavirus</subject>
<subject>viral helicase</subject>
<title>On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus</title>
<type>Article</type>
<identifier.openurl>http://library.hku.hk:4550/resserv?sid=HKU:IR&amp;issn=1742-464X&amp;volume=278&amp;issue=2&amp;spage=383&amp;epage=389&amp;date=2011&amp;atitle=On+the+mechanisms+of+bananin+activity+against+severe+acute+respiratory+syndrome+coronavirus</identifier.openurl>
<description.nature>Link_to_subscribed_fulltext</description.nature>
<identifier.doi>10.1111/j.1742-4658.2010.07961.x</identifier.doi>
<identifier.pmid>21134131</identifier.pmid>
<identifier.scopus>eid_2-s2.0-78651078154</identifier.scopus>
<identifier.hkuros>185117</identifier.hkuros>
<relation.references>http://www.scopus.com/mlt/select.url?eid=2-s2.0-78651078154&amp;selection=ref&amp;src=s&amp;origin=recordpage</relation.references>
<identifier.volume>278</identifier.volume>
<identifier.issue>2</identifier.issue>
<identifier.spage>383</identifier.spage>
<identifier.epage>389</identifier.epage>
<identifier.isi>WOS:000285877700018</identifier.isi>
<publisher.place>United Kingdom</publisher.place>
<relation.project>Helicases as antiviral drug targets</relation.project>
<relation.project>Determine the functions of the putative metal-binding domain of SARS-CoV helicase</relation.project>
<identifier.citeulike>8627024</identifier.citeulike>
</item>
Author Affiliations
  1. The University of Hong Kong
  2. SienaBiografix Srl
  3. HKU-Pasteur Research Centre
  4. Università degli Studi di Siena