Snake Venomic of Crotalus durissus terrificus—Correlation with Pharmacological Activities

Abstract

The snake venomic of Crotalus durissus terrificus was analyzed by 2-D and 1-D electrophoresis and subsequent MS/MS and enzymatic assays. The venomic of the South American rattlesnake comprises toxins from seven protein families: phospholipases A(2), serine proteinases, ecto-5'-nucleotidases, metalloproteinases, nerve growth factors, phosphodiesterases, and glutaminyl cyclase. The venom toxin composition correlates with the clinical manifestation of the crotalinae snake bites and explains pathological effects of the venom such as neurotoxicity, systemic myonecrosis, hemostatic disorders, myoglobinuria, and acute renal failure. The vast majority of toxins are potentially involved in neurotoxicity, myotoxicity, and coagulopathy. The predominant venom components are neurotoxic phospholipases A(2) and serine proteinases. The venom is a rich source of 5'-nucleotidases (7.8% of the identified toxins) inducing hemostatic disorders. Analysis of the venom protein composition provided a catalogue for secreted toxins. The venomic composition of Crotalus d. terrificus and venom gland transcriptome of the synonymous subspecies Crotalus d. collilineatus show differences in the occurrence of protein families and in the abundance of toxins. Some of the venom components identified by the proteomic analysis were not reported in the transcriptome of the Crotalus d. collilineatus venom gland. Enzymatic activities of the Crotalus d. terrificus venom were determined and correlated with the proteomic composition.

Elapid Snake Venom Analyses Show the Specificity of the Peptide Composition at the Level of Genera Naja and Notechis

“…It is known that the venom composition depends on the diet of the snake, the geographical region, ontogenetic variations, etc. ([17] and the references therein). Furthermore, very low quantities of the respective toxins in the venom can prevent their identification.…”

Strategies in ‘snake venomics’ aiming at an integrative view of compositional, functional, and immunological characteristics of venoms

“…Notwithstanding, these powerful strategies have thus far provided most often qualitative information on venom composition. It should be stressed that relative protein abundances reported in some studies based on this analytical pipeline [37, 38], as well as on the 2DE workflow [39, 40], correspond to ‘frequency of identification’, or ‘percentage of the protein sequences’, which may not be necessarily equivalent to abundance [41], and may therefore not reflect the actual quantitative distribution of components in the venom. Thus, in all peptide-based quantitation techniques, the assumption is made that protein digestion is complete, and that the resulting proteolytic peptides are equally detectable by the mass spectrometric technique used for the analysis.…”

Comparative venomics of the Prairie Rattlesnake (Crotalus viridis viridis) from Colorado: Identification of a novel pattern of ontogenetic changes in venom composition and assessment of the immunoreactivity of the commercial antivenom CroFab®

“…Produced and stored in a pair of highly specialized cephalic 67 gland, snake venoms represent a complex mixture of bioactive 68 proteins and peptides that exhibit diverse biochemical and 69 pharmacological functions [1]. Venoms likely evolved via the 70 co-opting and secondary modification of endogenous proteins 71 with normal physiological functions early in the evolution of 72 advanced snakes [e.g., 2 but see 3,4], enabling the transition from 73 a mechanical (constriction) to a chemical (venom) means of 74 subduing prey [5].…”