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

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

Author Azzolini, S. S. Google Scholar
Sasaki, S. D. Google Scholar
Torquato, J. S. Google Scholar
Andreotti, R. Google Scholar
Andreotti, E. Google Scholar
Tanaka, A. S. Google Scholar
Institution Universidade Federal de São Paulo (UNIFESP)
Empresa Brasileira de Pesquisa Agropecuária (EMBRAPA)
CTr Controle Zoonoses
Abstract Blood 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.
Keywords protease inhibitors
tick
protein purification
Rhipicephalus sanguineus
Language English
Date 2003-09-15
Published in Archives of Biochemistry and Biophysics. New York: Elsevier B.V., v. 417, n. 2, p. 176-182, 2003.
ISSN 0003-9861 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 176-182
Origin http://dx.doi.org/10.1016/S0003-9861(03)00344-8
Access rights Closed access
Type Article
Web of Science ID WOS:000185220500006
URI http://repositorio.unifesp.br/handle/11600/27415

Show full item record




File

File Size Format View

There are no files associated with this item.

This item appears in the following Collection(s)

Search


Browse

Statistics

My Account