Snake venom metalloproteinases (SVMPs) and
snake venom serine proteinases (SVSPs) are among the most abundant
enzymes in many
snake venoms, particularly among viperids. These
proteinases are responsible for some of the clinical manifestations classically seen in viperid envenomings, including
hemorrhage,
necrosis, and coagulopathies. The objective of this study was to investigate the enzymatic activities of these
proteins using a high-throughput
peptide library to screen for the
proteinase targets of the
venoms of five viperid (Echis carinatus, Bothrops asper, Daboia russelii, Bitis arietans, Bitis gabonica) and one elapid (Naja nigricollis) species of high medical importance. The
proteinase activities of these
venoms were each tested against 360
peptide substrates, yielding 2160 activity profiles. A nonlinear regression model that accurately described the observed enzymatic activities was fitted to the experimental data, allowing for the comparison of cleavage rates across species. In this study, previously unknown
protein targets of
snake venom proteinases were identified, potentially implicating novel human and animal
proteins that may be involved in the pathophysiology of viper envenomings. The functional relevance of these targets was further evaluated and discussed. These new findings may contribute to our understanding of the clinical manifestations and underlying biochemical mechanisms of
snakebite envenoming by viperid species.