Poliovirus 3C proteinase inhibition by organotelluranes

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dc.contributor.author Gouvea, Iuri E. [UNIFESP]
dc.contributor.author Santos, Jorge A. N. [UNIFESP]
dc.contributor.author Burlandy, Fernanda M.
dc.contributor.author Tersariol, Ivarne L. S.
dc.contributor.author Silva, Edson E. da
dc.contributor.author Juliano, Maria A. [UNIFESP]
dc.contributor.author Juliano, Luiz [UNIFESP]
dc.contributor.author Cunha, Rodrigo L. O. R. [UNIFESP]
dc.date.accessioned 2016-01-24T14:06:24Z
dc.date.available 2016-01-24T14:06:24Z
dc.date.issued 2011-04-01
dc.identifier http://dx.doi.org/10.1515/BC.2011.059
dc.identifier.citation Biological Chemistry. Berlin: Walter de Gruyter & Co, v. 392, n. 6, p. 587-591, 2011.
dc.identifier.issn 1431-6730
dc.identifier.uri http://repositorio.unifesp.br/handle/11600/33628
dc.description.abstract The 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.sponsorship Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
dc.description.sponsorship Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
dc.format.extent 587-591
dc.language.iso eng
dc.publisher Walter de Gruyter & Co
dc.relation.ispartof Biological Chemistry
dc.rights Acesso restrito
dc.subject antiviral en
dc.subject organotellurides en
dc.subject picornavirus en
dc.subject protease inhibitor en
dc.subject proteinase en
dc.subject tellurium en
dc.title Poliovirus 3C proteinase inhibition by organotelluranes en
dc.type Artigo
dc.contributor.institution Universidade Federal de São Paulo (UNIFESP)
dc.contributor.institution Inst Oswaldo Cruz
dc.contributor.institution Univ Mogi das Cruzes
dc.contributor.institution Universidade Federal do ABC (UFABC)
dc.description.affiliation Universidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.description.affiliation Inst Oswaldo Cruz, Fundacao Oswaldo Cruz, Dept Virol, BR-21045060 Rio de Janeiro, Brazil
dc.description.affiliation Univ Mogi das Cruzes, Ctr Interdisciplinar Invest Bioquim, BR-08780911 Mogi das Cruzes, SP, Brazil
dc.description.affiliation Univ Fed ABC, Ctr Cieencias Nat & Humanas, BR-09210580 Santo Andre, SP, Brazil
dc.description.affiliationUnifesp Universidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, BR-04044020 São Paulo, Brazil
dc.identifier.doi 10.1515/BC.2011.059
dc.description.source Web of Science
dc.identifier.wos WOS:000290715200010


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