Poliovirus 3C proteinase inhibition by organotelluranes

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dc.contributor.authorGouvea, Iuri E. [UNIFESP]
dc.contributor.authorSantos, Jorge A. N. [UNIFESP]
dc.contributor.authorBurlandy, Fernanda M.
dc.contributor.authorTersariol, Ivarne L. S.
dc.contributor.authorSilva, Edson E. da
dc.contributor.authorJuliano, Maria A. [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorCunha, Rodrigo L. O. R. [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionInst Oswaldo Cruz
dc.contributor.institutionUniv Mogi das Cruzes
dc.contributor.institutionUniversidade Federal do ABC (UFABC)
dc.date.accessioned2016-01-24T14:06:24Z
dc.date.available2016-01-24T14:06:24Z
dc.date.issued2011-04-01
dc.description.abstractThe 3C proteinase, essential for human poliovirus (PV) replication, has unique characteristics as its three-dimensional structure resembles chymotrypsin, but its catalytic nucleophile is a cysteine SH group rather than the OH group of serine. Here, we describe the use of tellurium compounds as inhibitors of PV3C proteinase. A rapid, stoichiometric and covalent inactivation of PV3C was observed with both a chloro-telluroxetane and a bis-vinylic organotellurane. These compounds also inhibit human cathepsins B, L, S, and K with second order rate constants higher than those obtained for PV3C. Chloro-telluroxetane inhibits replication of PV in human embryonic rhabdomyosarcoma cells in the low micromolar range and below the toxic level for the host cells. Bis-vinylic organotellurane is more effective as antiviral agent but reduces the cell viability by 20% at 10 mM, a concentration almost completely inhibiting virus growth. This is the first description of inhibition of viral 3C proteinase with antiviral property by this class of compounds.en
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliationInst Oswaldo Cruz, Fundacao Oswaldo Cruz, Dept Virol, BR-21045060 Rio de Janeiro, Brazil
dc.description.affiliationUniv Mogi das Cruzes, Ctr Interdisciplinar Invest Bioquim, BR-08780911 Mogi das Cruzes, SP, Brazil
dc.description.affiliationUniv Fed ABC, Ctr Cieencias Nat & Humanas, BR-09210580 Santo Andre, SP, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.sourceWeb of Science
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorshipConselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent587-591
dc.identifierhttp://dx.doi.org/10.1515/BC.2011.059
dc.identifier.citationBiological Chemistry. Berlin: Walter de Gruyter & Co, v. 392, n. 6, p. 587-591, 2011.
dc.identifier.doi10.1515/BC.2011.059
dc.identifier.issn1431-6730
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33628
dc.identifier.wosWOS:000290715200010
dc.language.isoeng
dc.publisherWalter de Gruyter & Co
dc.relation.ispartofBiological Chemistry
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.subjectantiviralen
dc.subjectorganotelluridesen
dc.subjectpicornavirusen
dc.subjectprotease inhibitoren
dc.subjectproteinaseen
dc.subjecttelluriumen
dc.titlePoliovirus 3C proteinase inhibition by organotelluranesen
dc.typeinfo:eu-repo/semantics/article
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