Yellow fever virus NS2B/NS3 protease: Hydrolytic Properties and Substrate Specificity

dc.contributor.authorKondo, Marcia Yuri [UNIFESP]
dc.contributor.authorOliveira, Lilian Caroline Gonçalves de [UNIFESP]
dc.contributor.authorOkamoto, Débora Noma [UNIFESP]
dc.contributor.authorAraujo, Marina R. T. de
dc.contributor.authorDuarte dos Santos, Claudia N.
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorGouvea, Iuri Estrada [UNIFESP]
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionInst Carlos Chagas Fiocruz PR
dc.date.accessioned2016-01-24T14:06:25Z
dc.date.available2016-01-24T14:06:25Z
dc.date.issued2011-04-22
dc.description.abstractHere we report the hydrolytic behavior of recombinant YFV NS2B/NS3 protease against FRET substrates mimicking the prime and non-prime region of the natural polyprotein cleavage sites. While the P2-P'1 motif is the main factor associated with the catalytic efficiency of Dengue (DV) and West Nile Virus (WNV) protease, we show that the k(cat)/K-m of YFV NS2B/NS3 varied by more than two orders of magnitude, despite the presence of the same motif in all natural substrates. the catalytic significance of this homogeneity - a unique feature among worldwide prominent flavivirus - was kinetically analyzed using FRET peptides containing all possible combinations of two and three basic amino acids in tandem, and Arg and Lys residues produced distinct effects on k(cat)/K-m. the parallel of our data with those obtained in vivo by Chambers et al. (1991) restrains the idea that these sites co-evolved with the NS2B/NS3 protease to promote highly efficient hydrolysis and supports the notion that secondary substrate interaction distant from cleavage sites are the main factor associated with the different hydrolytic rates on YFV NS2B-NS3pro natural substrates. (C) 2011 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Biophys, Escola Paulista Med, BR-04044020 São Paulo, Brazil
dc.description.affiliationInst Carlos Chagas Fiocruz PR, BR-81350010 Curitiba, Parana, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Biophys, Escola Paulista Med, 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.extent640-644
dc.identifierhttp://dx.doi.org/10.1016/j.bbrc.2011.03.054
dc.identifier.citationBiochemical and Biophysical Research Communications. San Diego: Academic Press Inc Elsevier Science, v. 407, n. 4, p. 640-644, 2011.
dc.identifier.doi10.1016/j.bbrc.2011.03.054
dc.identifier.fileWOS000290240500003.pdf
dc.identifier.issn0006-291X
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33639
dc.identifier.wosWOS:000290240500003
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofBiochemical and Biophysical Research Communications
dc.rightsAcesso aberto
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectFRET substrateen
dc.subjectEnzyme kineticsen
dc.subjectSerine-proteasesen
dc.subjectFlavivirusen
dc.subjectDengueen
dc.titleYellow fever virus NS2B/NS3 protease: Hydrolytic Properties and Substrate Specificityen
dc.typeArtigo
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