Article: On the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus

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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, O2 4
Bernini, A2 4
Zheng, BJ1
Niccolai, N2 4
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
2011 Impact Factor: 3.79
2011 SCImago Journal Rankings: 0.326
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 Field
Value
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.grantHelicases as antiviral drug targets
dc.description.grantDetermine the functions of the putative metal-binding domain of SARS-CoV helicase
dc.description.grantcode10167
dc.description.grantcode82104
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
2011 Impact Factor: 3.79
2011 SCImago Journal Rankings: 0.326
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.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
Author Affiliations
  1. The University of Hong Kong
  2. SienaBiografix Srl
  3. HKU-Pasteur Research Centre
  4. Università degli Studi di Siena