Abstract
BackgroundClassically, Crotalus durissus terrificus (Cdt) venom can be described, according to chromatographic criteria, as a simple venom, composed of four major toxins, namely: gyroxin, crotamine, crotoxin and convulxin. Crotoxin is a non-covalent heterodimeric neurotoxin constituted of two subunits: an active phospholipase A2 and a chaperone protein, termed crotapotin. This molecule is composed of three peptide chains connected by seven disulfide bridges. Naturally occurring variants/isoforms of either crotoxin or crotapotin itself have already been reported.MethodsThe crude Cdt venom was separated by using RP-HPLC and the toxins were identified by mass spectrometry (MS). Crotapotin was purified, reduced and alkylated in order to separate the peptide chains that were further analyzed by mass spectrometry and de novo peptide sequencing.ResultsThe RP-HPLC profile of the isolated crotapotin chains already indicated that the α chain would present isoforms, which was corroborated by the MS and tandem mass spectrometry analyses.ConclusionIt was possible to observe that the Cdt crotapotin displays a preferred amino acid substitution pattern present in the α chain, at positions 31 and 40. Moreover, substitutions could also be observed in β and γ chains (one for each). The combinations of these four different peptides, with the already described chains, would produce ten different crotapotins, which is compatible to our previous observations for the Cdt venom.
Highlights
Crotalus durissus terrificus (Cdt) venom can be described, according to chromatographic criteria, as a simple venom, composed of four major toxins, namely: gyroxin, crotamine, crotoxin and convulxin
The combinations of these four different peptides, with the already described chains, would produce ten different crotapotins, which is compatible to our previous observations for the Cdt venom
We have developed a method for the isolation and biochemical characterization of crotapotin from crude Cdt venom, including the chromatographic de Oliveira et al Journal of Venomous Animals and Toxins including Tropical Diseases (2017) 23:46 separation of the peptide chains after reduction and alkylation, and de novo mass spectrometry peptide sequencing
Summary
Crotalus durissus terrificus (Cdt) venom can be described, according to chromatographic criteria, as a simple venom, composed of four major toxins, namely: gyroxin, crotamine, crotoxin and convulxin. Crotoxin is a non-covalent heterodimeric neurotoxin constituted of two subunits: an active phospholipase A2 and a chaperone protein, termed crotapotin This molecule is composed of three peptide chains connected by seven disulfide bridges. Snake venoms are complex mixtures rich in proteins and peptides, in which such molecules can comprise up to 95% of the venom dry weight [1, 2] Such molecules do aid the animal survival, once they may be used either as a hunting tool or as a defense mechanism [3]. The major Crotalus durissus terrificus (Cdt) venom toxin, is the most toxic [5, 6] It is a heterodimeric neurotoxin comprised of a basic phospholipase A2 (PLA2) and an acidic protein, known as crotapotin [7, 8]. This peptide has been described as presenting anti-inflammatory activity and being able to modulate the humoral immunity, including in some neurodegenerative autoimmune disorders [13,14,15,16,17]
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