TY - JOUR
T1 - Proteomic and toxinological characterization of Peruvian pitviper Bothrops brazili (“jergón shushupe”), venom
AU - Rodrigues, Carolina Rego
AU - Molina, Denis Alexis Molina
AU - Silva de Assis, Thamyres C.
AU - Liberato, Camila
AU - Melo-Braga, Marcella N.
AU - Ferreyra, César Bonilla
AU - Cárdenas, Javier
AU - Costal-Oliveira, Fernanda
AU - Guerra-Duarte, Clara
AU - Chávez-Olórtegui, Carlos
N1 - Publisher Copyright:
© 2020 Elsevier Ltd
PY - 2020/9
Y1 - 2020/9
N2 - 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.
AB - 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.
KW - Amazonian region
KW - Bothropic venoms
KW - Bothrops brazili
KW - MALDI-TOF/TOF
KW - Proteomic analyses
UR - http://www.scopus.com/inward/record.url?scp=85085936197&partnerID=8YFLogxK
U2 - 10.1016/j.toxicon.2020.05.016
DO - 10.1016/j.toxicon.2020.05.016
M3 - Artículo
C2 - 32479836
AN - SCOPUS:85085936197
SN - 0041-0101
VL - 184
SP - 19
EP - 27
JO - Toxicon
JF - Toxicon
ER -