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(Referência obtida automaticamente do Web of Science, por meio da informação sobre o financiamento pela FAPESP e o número do processo correspondente, incluída na publicação pelos autores.)

Kn-Ba: a novel serine protease isolated from Bitis arietans snake venom with fibrinogenolytic and kinin-releasing activities

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Autor(es):
Amadeu Megale, Angela Alice [1] ; Magnoli, Fabio Carlos [1] ; Kuniyoshi, Alexandre Kazuo [1] ; Iwai, Leo Kei [2] ; Tambourgi, Denise V. [1] ; Portaro, Fernanda C. V. [1] ; da Silva, Wilmar Dias [1]
Número total de Autores: 7
Afiliação do(s) autor(es):
[1] Butantan Inst, Immunochem Lab, BR-05503900 Sao Paulo - Brazil
[2] Butantan Inst, Special Lab Appl Toxinol, Ctr Toxins Immune Response & Cell Signaling CeTIC, BR-05503900 Sao Paulo - Brazil
Número total de Afiliações: 2
Tipo de documento: Artigo Científico
Fonte: Journal of Venomous Animals and Toxins including Tropical Diseases; v. 24, DEC 13 2018.
Citações Web of Science: 1
Resumo

BackgroundBitis arietans is a venomous snake found in sub-Saharan Africa and in parts of Morocco and Saudi Arabia. The envenomation is characterized by local and systemic reactions including pain, blistering, edema and tissue damage, besides hemostatic and cardiovascular disturbances, which can cause death or permanent disabilities in its victims. However, the action mechanisms that provoke these effects remain poorly understood, especially the activities of purified venom components. Therefore, in order to elucidate the molecular mechanisms that make the Bitis arietans venom so potent and harmful to human beings, this study reports the isolation and biochemical characterization of a snake venom serine protease (SVSP).MethodsSolubilized venom was fractionated by molecular exclusion chromatography and the proteolytic activity was determined using fluorescent substrates. The peaks that showed serine protease activity were determined by blocking the proteolytic activity with site-directed inhibitors. In sequence, the fraction of interest was submitted to another cycle of molecular exclusion chromatography. The purified serine protease was identified by mass spectrometry and characterized biochemically and immunochemically.ResultsA serine protease of 33kDa with fibrinogen-degrading and kinin-releasing activities was isolated, described, and designated herein as Kn-Ba. The experimental Butantan Institute antivenom produced against Bitis arietans venom inhibited the Kn-Ba activity.ConclusionsThe in vitro activities of Kn-Ba can be correlated with the capacity of the venom to provoke bleeding and clotting disorders as well as hypotension, which are common symptoms presented by envenomed victims. Obtaining satisfactory Kn-Ba inhibition through the experimental antivenom is important, given the WHO's recommendation of immunotherapy in cases of human accidents with venomous snakes. (AU)

Processo FAPESP: 13/07467-1 - CeTICS - Centro de Toxinas, Imuno-Resposta e Sinalização Celular
Beneficiário:Hugo Aguirre Armelin
Linha de fomento: Auxílio à Pesquisa - Centros de Pesquisa, Inovação e Difusão - CEPIDs
Processo FAPESP: 13/15344-7 - Eficácia do soro antibotrópico produzido no Instituto Butantan: obtenção, caracterização e neutralização de serinopeptidases de interesse do veneno de Bothrops Jararaca
Beneficiário:Alexandre Kazuo Kuniyoshi
Linha de fomento: Bolsas no Brasil - Doutorado
Processo FAPESP: 15/15364-3 - Análise do potencial tóxico de proteases e peptídeos presentes no veneno do escorpião Tityus serrulatus e do poder neutralizante dos antivenenos comerciais: aprimorando o conhecimento do veneno e seu mecanismo de ação
Beneficiário:Fernanda Calheta Vieira Portaro
Linha de fomento: Auxílio à Pesquisa - Regular