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dc.contributor.authorPorcino, Gabriane Nascimento
dc.contributor.authorCarvalho-Campos, Cristiane
dc.contributor.authorRibeiro Gomes Maia, Ana Carolina
dc.contributor.authorDetoni, Michelle Lima
dc.contributor.authorFaria-Pinto, Priscila
dc.contributor.authorCoimbra, Elaine Soares
dc.contributor.authorMarques, Marcos Jose
dc.contributor.authorJuliano, Maria Aparecida [UNIFESP]
dc.contributor.authorJuliano, Luiz [UNIFESP]
dc.contributor.authorDiniz, Vanessa Alvaro
dc.contributor.authorCorte-Real, Suzana
dc.contributor.authorVasconcelos, Eveline Gomes
dc.date.accessioned2016-01-24T14:27:43Z
dc.date.available2016-01-24T14:27:43Z
dc.date.issued2012-10-01
dc.identifierhttp://dx.doi.org/10.1016/j.exppara.2012.08.009
dc.identifier.citationExperimental Parasitology. San Diego: Academic Press Inc Elsevier Science, v. 132, n. 2, p. 293-299, 2012.
dc.identifier.issn0014-4894
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/35295
dc.description.abstractNucleoside triphosphate diphosphohydrolase (NTPDase) activity was recently characterized in Leishmania (Viannia) braziliensis promastigotes (Lb), and an antigenic conserved domain (r82-121) from the specific NTPDase 1 isoform was identified. in this work, mouse polyclonal antibodies produced against two synthetic peptides derived from this domain (LbB1LJ, r82-103; LbB2LJ, r102-121) were used. the anti-LbB1LJ or anti-LbB2LJ antibodies were immobilized on protein A-sepharose and immunoprecipitated the NTPDase 1 of 48 kDa and depleted approximately 40% of the phosphohydrolytic activity from detergent-homogenized Lb preparation. Ultrastructural immunocytochemical microscopy identified the NTPDase 1 on the parasite surface and in its subcellular cytoplasmic vesicles, mitochondria, kinetoplast and nucleus. the ATPase and ADPase activities of detergent-homogenized Lb preparation were partially inhibited by anti-LbB1LJ antibody (43-79%), which was more effective than that inhibition (18-47%) by anti-LbB2LJ antibody. in addition, the immune serum anti-LbB1LJ (67%) or anti-LbB2LJ (33%) was cytotoxic, significantly reducing the promastigotes growth in vitro. the results appoint the conserved domain from the L braziliensis NTPDase as an important target for inhibitor design and the potential application of these biomolecules in experimental protocols of disease control. (c) 2012 Elsevier Inc. All rights reserved.en
dc.description.sponsorshipFundação de Amparo à Pesquisa do Estado de Minas Gerais (FAPEMIG)
dc.description.sponsorshipPROQUALI/UFJF
dc.description.sponsorshipCoordenação de Aperfeiçoamento de Pessoal de Nível Superior (CAPES)
dc.format.extent293-299
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofExperimental Parasitology
dc.rightsAcesso aberto
dc.subjectApyraseen
dc.subjectATP diphosphohydrolaseen
dc.subjectNTPaseen
dc.subjectPeptideen
dc.subjectLeishmaniasisen
dc.subjectImmunocytochemicalen
dc.titleLeishmania (Viannia) braziliensis nucleoside triphosphate diphosphohydrolase (NTPDase 1): Localization and in vitro inhibition of promastigotes growth by polyclonal antibodiesen
dc.typeArtigo
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.contributor.institutionUniv Fed Juiz de Fora
dc.contributor.institutionUniv Fed Alfenas
dc.contributor.institutionFiocruz MS
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.description.affiliationUniv Fed Juiz de Fora, Inst Ciencias Biol, Dept Bioquim, BR-36036900 Juiz de Fora, MG, Brazil
dc.description.affiliationUniv Fed Alfenas, Inst Ciencias Biomed, Dept Ciencias Biol, Alfenas, MG, Brazil
dc.description.affiliationFiocruz MS, Inst Oswaldo Cruz, Lab Biol Estrut, Rio de Janeiro, RJ, Brazil
dc.description.affiliationUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, São Paulo, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Escola Paulista Med, Dept Biofis, São Paulo, Brazil
dc.description.sponsorshipIDFAPEMIG: CBB-APQ-01384-09
dc.description.sponsorshipIDFAPEMIG: CBB-APQ 00754-09
dc.identifier.fileWOS000309737900027.pdf
dc.identifier.doi10.1016/j.exppara.2012.08.009
dc.description.sourceWeb of Science
dc.identifier.wosWOS:000309737900027


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