Rhipicephalus sanguineus trypsin inhibitors present in the tick larvae: isolation, characterization, and partial primary structure determination

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dc.contributor.authorAzzolini, S. S.
dc.contributor.authorSasaki, S. D.
dc.contributor.authorTorquato, J. S.
dc.contributor.authorAndreotti, R.
dc.contributor.authorAndreotti, E.
dc.contributor.authorTanaka, A. S.
dc.contributor.institutionUniversidade Federal de São Paulo (UNIFESP)
dc.contributor.institutionEmpresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
dc.contributor.institutionCTr Controle Zoonoses
dc.date.accessioned2016-01-24T12:34:03Z
dc.date.available2016-01-24T12:34:03Z
dc.date.issued2003-09-15
dc.description.abstractBlood sucking animals are a rich source of proteinase inhibitors mainly those that interfere in their host hemostatic systems. the tick Rhipicephalus sanguineus is an ectoparasite of dogs and other animals. the aims of this work were the purification and characterization of serine proteinase inhibitors present in R. sanguineus larvae (RsTI). the inhibitors (RsTI) were isolated by affinity chromatography on trypsin-Sepharose and ion exchange chromatographies in Resource Q and Mono S columns. These RsTIs were separated in around 12 different protein peaks, when they showed molecular masses between 8 and 18 kDa, by SDS-PAGE. Purified RsTIs presented differences in the specificity for different serine proteinases. RsTIQ2 was, better inhibitor than RsTIQ7 and RsTIS5 for neutrophil elastase, plasmin, and HuPK with dissociation constants (K-i) of 1.3, 3.2, and 22 nM, respectively. Other inhibitors such as RsTIQ7, RsTIS3, and RsTIS5 also affected neutrophil elastase and plasmin with K-i in the nM range. the RsTIQ2, RsTIQ7, and RsTIS5 amino acid sequence data allowed classifying them as members of the Kunitz-type serine proteinase inhibitor family, even though the RsTI role is still unknown. Our present results showed that serine proteinase inhibitors from R. sanguineus are similar to inhibitors from Boophilus microplus other hard tick species, suggesting a similar role of these inhibitors in hard tick species and also as a potential tool to generate or improve vaccine against different ectoparasites with an unique antigen. (C) 2003 Elsevier Inc. All rights reserved.en
dc.description.affiliationUniversidade Federal de São Paulo, Dept Bioquim, Escola Paulista Med, BR-04044020 São Paulo, SP, Brazil
dc.description.affiliationCNPGC, EMBRAPA, Campo Grande, MS, Brazil
dc.description.affiliationCTr Controle Zoonoses, Prefeitura Municipal, Campo Grande, MS, Brazil
dc.description.affiliationUnifespUniversidade Federal de São Paulo, Dept Bioquim, Escola Paulista Med, BR-04044020 São Paulo, SP, Brazil
dc.description.sourceWeb of Science
dc.format.extent176-182
dc.identifierhttp://dx.doi.org/10.1016/S0003-9861(03)00344-8
dc.identifier.citationArchives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 417, n. 2, p. 176-182, 2003.
dc.identifier.doi10.1016/S0003-9861(03)00344-8
dc.identifier.issn0003-9861
dc.identifier.urihttp://repositorio.unifesp.br/handle/11600/27415
dc.identifier.wosWOS:000185220500006
dc.language.isoeng
dc.publisherElsevier B.V.
dc.relation.ispartofArchives of Biochemistry and Biophysics
dc.rightsAcesso restrito
dc.rights.licensehttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.subjectprotease inhibitorsen
dc.subjectticken
dc.subjectprotein purificationen
dc.subjectRhipicephalus sanguineusen
dc.titleRhipicephalus sanguineus trypsin inhibitors present in the tick larvae: isolation, characterization, and partial primary structure determinationen
dc.typeArtigo
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