Abstract
Myotoxic phospholipases A2 (PLA2) are responsible for many clinical manifestations in envenomation by Bothrops snakes. A new myotoxic acidic Asp49 PLA2 (BaCol PLA2) was isolated from Colombian Bothrops asper venom using reverse-phase high performance liquid chromatography (RP-HPLC). BaCol PLA2 had a molecular mass of 14,180.69 Da (by mass spectrometry) and an isoelectric point of 4.4. The complete amino acid sequence was obtained by cDNA cloning (GenBank accession No. MF319968) and revealed a mature product of 124 amino acids with Asp at position 49. BaCol PLA2 showed structural homology with other acidic PLA2 isolated from Bothrops venoms, including a non-myotoxic PLA2 from Costa Rican B. asper. In vitro studies showed cell membrane damage without exposure of phosphatidylserine, an early apoptosis hallmark. BaCol PLA2 had high indirect hemolytic activity and moderate anticoagulant action. In mice, BaCol PLA2 caused marked edema and myotoxicity, the latter seen as an increase in plasma creatine kinase and histological damage to gastrocnemius muscle fibers that included vacuolization and hyalinization necrosis of the sarcoplasm.
Highlights
Colombia has the third highest biodiversity of snakes in the Americas [1]
Many acidic phospholipases A2 (PLA2) isolated from snake venoms are devoid of pharmacological activities or toxicity, Many acidic PLA2 isolated from snake venoms are devoid of pharmacological activities or including myotoxicity [11,14,15]
We describe the structural and functional of BaCol PLA2, a new acidic myotoxic Asp49 PLA2 isolated from Colombian B. asper venom
Summary
Colombia has the third highest biodiversity of snakes in the Americas [1]. 94.6% of the snakebites are caused by snakes of the genus Bothrops [2]. In Colombia, Bothrops asper is found in the Pacific, Caribbean and Andean (western slopes) regions where it accounts for 50–80% of snakebites [2]. Envenomation by B. asper leads to sequelae in 6–10% of cases [2,3], with the most important being the loss of muscle mass leading to limb. The main toxins implicated in these effects are snake venom metalloproteinases (SVMPs) and PLA2 s [4,5]. Proteomic analyses have shown that B. asper venom contains at least seven protein families including disintegrin, phospholipases A2 , serine proteinases, C-type lectins, cysteine-rich secretory proteins (CRISP), L-amino acid oxidase, and Zn2+ -dependent metalloproteinases of which
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