Abstract
Feae’s viper Azemipos feae belongs to the Azemiopinae subfamily of the Viperidae family. The effects of Viperidae venoms are mostly coagulopathic with limited neurotoxicity manifested by phospholipases A2. From A. feae venom, we have earlier isolated azemiopsin, a novel neurotoxin inhibiting the nicotinic acetylcholine receptor. To characterize other A. feae toxins, we applied label-free quantitative proteomics, which revealed 120 unique proteins, the most abundant being serine proteinases and phospholipases A2. In total, toxins representing 14 families were identified, among which bradykinin-potentiating peptides with unique amino acid sequences possessed biological activity in vivo. The proteomic analysis revealed also basal (commonly known as non-conventional) three-finger toxins belonging to the group of those possessing neurotoxic activity. This is the first indication of the presence of three-finger neurotoxins in viper venom. In parallel, the transcriptomic analysis of venom gland performed by Illumina next-generation sequencing further revealed 206 putative venom transcripts. Together, the study unveiled the venom proteome and venom gland transciptome of A. feae, which in general resemble those of other snakes from the Viperidae family. However, new toxins not found earlier in viper venom and including three-finger toxins and unusual bradykinin-potentiating peptides were discovered.
Highlights
Snake venoms are complex mixtures of peptides and proteins that are evolved in the process of evolution for protection from predators and for hunting
We have described the comprehensive venom-gland transcriptomic and quantitative proteomic venom characterization of A. feae viper
The proteomic analysis revealed three-finger toxins which belong to the group of non-conventional toxins possessing neurotoxic activity
Summary
Snake venoms are complex mixtures of peptides and proteins that are evolved in the process of evolution for protection from predators and for hunting. Three PLA2s were isolated from A. feae venom, and two of them contained. Natriuretic-peptide precursors contain sequences of a unique peptide neurotoxin, which was isolated by us from the venom and called azemiopsin [15]. By its capacity to block the nicotinic acetylcholine receptor, azemiopsin resembles waglerin, a disulfide-containing peptide from the Tropedolaemus wagleri venom, shares with it a homologous C-terminal hexapeptide and may be considered as a waglerin ancestor. These peptide neurotoxins are not typical for Viperidae venom. About 70 toxins representing 14 toxins families were identified; among them, new toxins not found earlier in viper venom and including three-finger toxins and unusual bradykinin-potentiating peptides were discovered
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