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.

Bothrops brazili是一名来自亚马逊地区的赌徒，在秘鲁造成了许多事故。尽管具有相关性，但其毒液尚未得到广泛表征。在目前的工作中，通过RP-HPLC，SDS-PAGE和MALDI-TOF / TOF分析了Broprops巴西蛇毒（Bb V）成分。鉴定出约37种蛋白质，属于7个家族。蛇毒金属蛋白酶（SVMPs）是毒液（33.05％），其次是蛇毒丝氨酸蛋白酶（SVSPs，26.11％）的最丰富的蛋白质，磷脂酶甲₂（PLA ₂，25.57％），蛇C型凝集素（CTL的（9.61％），L-氨基酸氧化酶（LAAO，3.80％），富含半胱氨酸的分泌蛋白（CRISP，1.67％）和缓激肽增强肽（BPP，0.20％）。体外与其他同功毒液相比，Bb V的酶促活性显示出高水平的SVMP活性和降低的Hyal活性。此外，Bb V降低了VERO细胞的活力。ELISA和Western Blotting显示，秘鲁和巴西的两性抗蛇毒素都能够识别Bb V成分。这项工作提供了对Bb V毒液含量的概述，并指出了秘鲁和巴西抗蛇毒动物处理该物种事故的潜在效率。