Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom

Carolina Rego Rodrigues, Denis Alexis Molina Molina, Thamyres C. Silva de Assis, Camila Liberato, Marcella N. Melo-Braga, César Bonilla Ferreyra, Javier Cárdenas, Fernanda Costal-Oliveira, Clara Guerra-Duarte, Carlos Chávez-Olórtegui

Producción científica: Contribución a una revistaArtículorevisión exhaustiva

5 Citas (Scopus)


Bothrops brazili is a pitviper from Amazonian region, responsible for many accidents in Peru. Despite its relevance, its venom has not been extensively characterized. In the present work, Bothrops brazili venom (BbV) components were analyzed by RP-HPLC, SDS-PAGE and MALDI-TOF/TOF. Approximately 37 proteins were identified, belonging to 7 families. Snake venom metalloproteinases (SVMPs) were the most abundant proteins of the venom (33.05%), followed by snake venom serine proteinases (SVSPs, 26.11%), phospholipases A2 (PLA2, 25.57%), snake C-type lectins (CTLs, 9.61%), L-aminoacid oxidase (LAAO, 3.80%), cystein-rich secretory proteins (CRISP, 1.67%) and Bradykinin-potentiating peptide (BPP, 0.20%). In vitro enzymatic activities of BbV showed high levels of SVMP activity and reduced Hyal activity in comparison with other bothropic venoms. Furthermore, BbV reduced VERO cells viability. ELISA and Western Blotting showed that both Peruvian and Brazilian bothropic antivenoms were able to recognize BbV components. This work provides an overview of BbV venom content and indicates a potential efficiency of Peruvian and Brazilian antivenoms to treat accidents with this species.

Idioma originalInglés
Páginas (desde-hasta)19-27
Número de páginas9
EstadoPublicada - set. 2020

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© 2020 Elsevier Ltd


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