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

TitleOn the mechanisms of bananin activity against severe acute respiratory syndrome coronavirus
Authors
Keywordsantiviral drugs
bananin
coronavirus
viral helicase
Issue Date2011
PublisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/
Citation
Febs Journal, 2011, v. 278 n. 2, p. 383-389 How to Cite?
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. © 2010 FEBS.
Persistent Identifierhttp://hdl.handle.net/10722/133580
ISSN
2013 Impact Factor: 3.986
2013 SCImago Journal Rankings: 2.131
ISI Accession Number ID
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.

References
Grants

 

Author Affiliations
  1. The University of Hong Kong
  2. SienaBiografix Srl
  3. HKU-Pasteur Research Centre
  4. Università degli Studi di Siena
DC FieldValueLanguage
dc.contributor.authorWang, Zen_HK
dc.contributor.authorHuang, JDen_HK
dc.contributor.authorWong, KLen_HK
dc.contributor.authorWang, PGen_HK
dc.contributor.authorZhang, HJen_HK
dc.contributor.authorTanner, JAen_HK
dc.contributor.authorSpiga, Oen_HK
dc.contributor.authorBernini, Aen_HK
dc.contributor.authorZheng, BJen_HK
dc.contributor.authorNiccolai, Nen_HK
dc.date.accessioned2011-05-24T02:11:17Z-
dc.date.available2011-05-24T02:11:17Z-
dc.date.issued2011en_HK
dc.identifier.citationFebs Journal, 2011, v. 278 n. 2, p. 383-389en_HK
dc.identifier.issn1742-464Xen_HK
dc.identifier.urihttp://hdl.handle.net/10722/133580-
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.en_HK
dc.languageengen_US
dc.publisherWiley-Blackwell Publishing Ltd.. The Journal's web site is located at http://www.febsjournal.org/en_HK
dc.relation.ispartofFEBS Journalen_HK
dc.rightsThe definitive version is available at www.blackwell-synergy.com-
dc.subjectantiviral drugsen_HK
dc.subjectbananinen_HK
dc.subjectcoronavirusen_HK
dc.subjectviral helicaseen_HK
dc.titleOn the mechanisms of bananin activity against severe acute respiratory syndrome coronavirusen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=1742-464X&volume=278&issue=2&spage=383&epage=389&date=2011&atitle=On+the+mechanisms+of+bananin+activity+against+severe+acute+respiratory+syndrome+coronavirus-
dc.identifier.emailHuang, JD:jdhuang@hkucc.hku.hken_HK
dc.identifier.emailTanner, JA:jatanner@hku.hken_HK
dc.identifier.emailZheng, BJ:bzheng@hkucc.hku.hken_HK
dc.identifier.authorityHuang, JD=rp00451en_HK
dc.identifier.authorityTanner, JA=rp00495en_HK
dc.identifier.authorityZheng, BJ=rp00353en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1111/j.1742-4658.2010.07961.xen_HK
dc.identifier.pmid21134131en_HK
dc.identifier.scopuseid_2-s2.0-78651078154en_HK
dc.identifier.hkuros185117en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-78651078154&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume278en_HK
dc.identifier.issue2en_HK
dc.identifier.spage383en_HK
dc.identifier.epage389en_HK
dc.identifier.isiWOS:000285877700018-
dc.publisher.placeUnited Kingdomen_HK
dc.relation.projectHelicases as antiviral drug targets-
dc.relation.projectDetermine the functions of the putative metal-binding domain of SARS-CoV helicase-
dc.identifier.scopusauthoridWang, Z=40162656400en_HK
dc.identifier.scopusauthoridHuang, JD=8108660600en_HK
dc.identifier.scopusauthoridWong, KL=7404758889en_HK
dc.identifier.scopusauthoridWang, PG=35749077000en_HK
dc.identifier.scopusauthoridZhang, HJ=53065015600en_HK
dc.identifier.scopusauthoridTanner, JA=35513993000en_HK
dc.identifier.scopusauthoridSpiga, O=6603012863en_HK
dc.identifier.scopusauthoridBernini, A=7004103621en_HK
dc.identifier.scopusauthoridZheng, BJ=7201780588en_HK
dc.identifier.scopusauthoridNiccolai, N=7003440494en_HK
dc.identifier.citeulike8627024-

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