Leishmania amazonensis META2 protein confers protection against heat shock and oxidative stress

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dc.contributor.authorRamos, Camila S.
dc.contributor.authorYokoyama-Yasunaka, Jenicer K. U.
dc.contributor.authorGuerra-Giraldez, Cristina
dc.contributor.authorPrice, Helen P.
dc.contributor.authorMortara, Renato A. [UNIFESP]
dc.contributor.authorSmith, Deborah F.
dc.contributor.authorUliana, Silvia R. B.
dc.contributor.institutionUniversidade de São Paulo (USP)
dc.contributor.institutionUniv York
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.date.accessioned2016-01-24T14:05:58Z
dc.date.available2016-01-24T14:05:58Z
dc.date.issued2011-01-01
dc.description.abstractThe META cluster of Leishmania amazonensis contains both META1 and META2 genes, which are upregulated in metacyclic promastigotes and encode proteins containing the META domain. Previous studies defined META2 as a 48.0-kDa protein, which is conserved in other Leishmania species and in Trypanosoma brucei. in this work, we demonstrate that META2 protein expression is regulated during the Leishmania life cycle but constitutive in T. brucei. META2 protein is present in the cytoplasm and flagellum of L amazonensis promastigotes. Leishmania META2-null replacement mutants are more sensitive to oxidative stress and, upon heat shock, assume rounded morphology with shortened flagella. the increased susceptibility of null parasites to heat shock is reversed by extra-chromosomal expression of the META2 gene. Defective Leishmania promastigotes exhibit decreased ability to survive in macrophages. By contrast, META2 expression is decreased by 80% in RNAi-induced T. brucei bloodstream forms with no measurable effect on survival or resistance to heat shock. (C) 2010 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniv São Paulo, Inst Ciencias Biomed, Dept Parasitol, BR-05508900 São Paulo, Brazil
dc.description.affiliationUniv York, Dept Biol, Ctr Immunol & Infect, York YO10 5DD, N Yorkshire, England
dc.description.affiliationUniv York, Hull York Med Sch, York YO10 5DD, N Yorkshire, England
dc.description.affiliationUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Microbiol Imunol & Parasitol, 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.extent228-237
dc.identifierhttp://dx.doi.org/10.1016/j.exppara.2010.08.004
dc.identifier.citationExperimental Parasitology. San Diego: Academic Press Inc Elsevier Science, v. 127, n. 1, p. 228-237, 2011.
dc.identifier.doi10.1016/j.exppara.2010.08.004
dc.identifier.issn0014-4894
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/33277
dc.identifier.wosWOS:000286486800036
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofExperimental Parasitology
dc.rightsinfo:eu-repo/semantics/restrictedAccess
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectLeishmania amazonensisen
dc.subjectMetacyclogenesisen
dc.subjectOxidative stressen
dc.subjectHeat shocken
dc.subjectCalpain-likeen
dc.subjectTrypanosoma bruceien
dc.titleLeishmania amazonensis META2 protein confers protection against heat shock and oxidative stressen
dc.typeinfo:eu-repo/semantics/article
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