Angiotensin-degrading serine peptidase: A new chymotrypsin-like activity in the venom of Bothrops jararaca partially blocked by the commercial antivenom

Angiotensin-degrading serine peptidase: A new chymotrypsin-like activity in the venom of Bothrops jararaca partially blocked by the commercial antivenom

Author Kuniyoshi, Alexandre Kazuo Google Scholar
Rocha, Marisa Google Scholar
Carvalho, Daniela Cajado Google Scholar
Juliano, Maria Aparecida Autor UNIFESP Google Scholar
Juliano, Luiz Autor UNIFESP Google Scholar
Tambourgi, Denise Vilarinho Google Scholar
Portaro, Fernanda Calheta Vieira Autor UNIFESP Google Scholar
Institution Butantan Inst
Universidade Federal de São Paulo (UNIFESP)
Abstract Snakebite envenomation is considered a highly relevant public health hazard in South America, having an impact in terms of mortality and morbidity. in Brazil, Bothrops (sensu latu) poisoning is responsible for 90% of the snakebites and in patients treated at the Vital Brazil Hospital (Butantan Institute) this index reaches 97.5%. the objective of the present study was to analyze more specifically the ability of the antibothropic antivenom, produced by the Butantan Institute, São Paulo, Brazil, to neutralize metallo-and serine peptidases, known as the major toxins present in Bothrops jararaca venom. A set of Fret peptides (Free Ressonance Energy Transfer) was studied using the BjV (B. jararaca venom) and site-directed inhibitors PMSF, EDTA and 1,10-phenanthroline. Two substrates were reached to be used as specific tools for studies with metallo peptidases, Abz-FASSAQ-EDDnp, and the serine peptidases, Abz-RPPGFSPFRQ-EDDnp. in disagreement with the literature, the use of both substrates and the antibothropic serum showed a weak neutralization of the serine peptidases present in this venom and a strong neutralization of the metallo peptidases. in order to investigate possible mechanisms of action that have not yet been described for the serine peptidases from the BjV, the present study shows for the first time a new tyrosine-specific chymotrypsin-like and angiotensin-degrading serine peptidase activity, that was partially blocked by the antibothropic serum. in conclusion, the antivenom presented a good neutralization of metallo peptidases but not of serine peptidases, indicating that further studies about serine peptidases immunogenicity are necessary to improve the antibothropic serum. (C) 2011 Elsevier B.V. All rights reserved.
Keywords Bothrops jararaca
Angiotensin I
Serine peptidases
Antivenom
Neglected disease
Language English
Sponsor Fundação de Amparo à Pesquisa do Estado de São Paulo (FAPESP)
Conselho Nacional de Desenvolvimento Científico e Tecnológico (CNPq)
Secretaria do Estado da Saude
Grant number FAPESP: 2008/028990-2
Date 2012-01-01
Published in Toxicon. Oxford: Pergamon-Elsevier B.V., v. 59, n. 1, p. 124-131, 2012.
ISSN 0041-0101 (Sherpa/Romeo, impact factor)
Publisher Elsevier B.V.
Extent 124-131
Origin http://dx.doi.org/10.1016/j.toxicon.2011.11.001
Access rights Open access Open Access
Type Article
Web of Science ID WOS:000300137300016
URI http://repositorio.unifesp.br/handle/11600/34342

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