Chapter 209 - Bothrops asper Metalloproteinase BaP1

Abstract

BaP1 is a class P-I hemorrhagic metalloproteinase isolated from the venom of Bothrops asper, a species responsible for most snakebite envenomations in Central America. This 22.7 kDa enzyme contains the catalytic motif HEXXHXXGXXH, characteristic of metzincins, and exhibits high affinity for extracellular matrix proteins such as type IV collagen, fibronectin, laminin, and fibrinogen. Its proteolytic activity weakens the capillary basement membrane, causing hemorrhage, muscle necrosis, edema, and local inflammation. The hemorrhagic mechanism of BaP1 involves the degradation of vascular components followed by capillary rupture due to hemodynamic forces. Additionally, BaP1 promotes complement activation and the release of proinflammatory cytokines, contributing to pain and local tissue damage. BaP1 is considered a key biological model for understanding the mechanisms of action of viperid snake venom metalloproteinases and for the development of adjunct therapies to conventional antivenom treatment.