Meeting Abstract
Snake venoms are highly variable, and their variation and rapid evolution—possibly driven by external factors such as environment and diet—make them fascinating phenotypic characters with human health implications. Because anti-venom is generally produced using venom from captive animals, understanding the effects of captivity on venom composition is important. We evaluated venom proteins from long-term (LT) captive and recently wild-caught (RC) eastern brown snakes, Pseudonaja textilis, utilizing protein gel electrophoresis, HPLC-MS, and shotgun proteomics by HPLC-tandem MS. We evaluated twelve (6 LT and 6 RC) individual venoms of snakes from South Australia. We identified proteins belonging to the three-finger toxin, cysteine-rich secretory protein, factor V-like and factor X-like subunits of the group C prothrombin activator, Kunitz-type serine protease inhibitor, phospholipases A2, and snake venom C-type lectin-like protein families, among others. Although crude venom HPLC analysis showed long-term captives to have higher amounts of some small molecular weight proteins, presence/absence patterns showed no correlation with time in captivity. Shotgun proteomic analyses indicate similar toxin family types across individuals, but with variation in isoforms present. These results indicate that captivity may have limited to no effect on venom composition, that venom diversity is high even within the same species, and that individuals from the same geographic region tend to have more similar venoms.
