Proteomic and toxicological profiling of the venom of Bothrocophias campbelli, a pitviper species from Ecuador and Colombia.

Detailed snake venom proteomes for nearly a hundred species in different pitviper genera have accumulated using 'venomics' methodologies. However, venom composition for some lineages remains poorly known. Bothrocophias (toad-headed pitvipers) is a genus restricted to the northwestern portion of South America for which information on venom composition is lacking. Here, we describe the protein composition, toxicological profiling, and antivenom neutralization of the venom of Bothrocophias campbelli, a species distributed in Colombia and Ecuador. Our analyses show that its venom mainly consists of phospholipases A2 (43.1%), serine proteinases (21.3%), and metalloproteinases (15.8%). The low proportion of metalloproteinases and high amount of a Lys49 phospholipase A2 homologue correlate well with the low hemorrhagic and high myotoxic effects found. Overall, B. campbelli venom showed a simpler composition compared to other crotalines in the region. A polyvalent antivenom prepared with a mixture of Bothrops asper, Crotalus simus, and Lachesis stenophrys venoms cross-recognized B. campbelli venom and neutralized its lethal effect in mice, albeit with a lower potency than for B. asper venom. Additional work comparing B. campbelli venom properties with those of related species could help understand the evolution of different venom protein families during the South American radiation of New World pitvipers.