Snake venomics ofBothrops punctatus, a semiarboreal pitviper species from Antioquia, Colombia

Abstract

Bothrops punctatus is an endangered, semi-arboreal pitviper species distributed in Panamá, Colombia, and Ecuador, whose venom is poorly characterized. In the present work, the protein composition of this venom was profiled using the ‘snake venomics’ analytical strategy. Decomplexation of the crude venom by RP-HPLC and SDS-PAGE, followed by tandem mass spectrometry of tryptic digests, showed that it consists of proteins assigned to at least nine snake toxin families. Metalloproteinases are predominant in this secretion (41.5% of the total proteins), followed by C-type lectin/lectin-like proteins (16.7%), bradykinin-potentiating peptides (10.7%), phospholipases A2 (93%), serine proteinases (5.4%), disintegrins (38%), L-amino acid oxidases (3.1%), vascular endothelial growth factors (17%), and cysteine-rich secretory proteins (1.2%). Altogether, 6.6% of the proteins were not identified. In vitro, the venom exhibited proteolytic, phospholipase A2, and L-amino acid oxidase activities, as well as angiotensin-converting enzyme (ACE)-inhibitory activity, in agreement with the obtained proteomic profile. Cytotoxic activity on murine C2C12 myoblasts was negative, suggesting that the majority of venom phospholipases A2 likely belong to the acidic type, which often lack major toxic effects. The protein composition of B. punctatus venom shows a good correlation with toxic activities here and previously reported, and adds further data in support of the wide diversity of strategies that have evolved in snake venoms to subdue prey, as increasingly being revealed by proteomic analyses.

Snake Venomics and Antivenomics of Bothrops diporus, a Medically Important Pitviper in Northeastern Argentina

“…In certain Crotalinae genera, such as Bothriechis , little correlation between phylogenetic signal and venom evolvability has been reported [ 69 , 70 , 71 , 72 ]. However, the venomic and antivenomic analyses of B. diporus are in line with the reported large protein family compositional conservation across many Bothrops taxa, which is also reflected in their extensive cross-immunoreactivity against different antivenoms generated using different Bothrops venoms [ 20 , 22 , 23 , 42 , 73 , 74 , 75 , 76 , 77 , 78 , 79 , 80 , 81 , 82 ]. This remarkable preservation across Bothrops during their ~14 million years of evolution [ 83 ] points to the possibility of generating broad-spectrum bothropic antivenoms covering all the classes of medically relevant toxins.…”

Proteomic Analyses of the Unexplored Sea Anemone Bunodactis verrucosa

“…A methodology based on shotgun analysis was employed to investigate the whole-body proteome of B. verrucosa . This methodology has been previously reported as suitable for diverse purposes related to protein identification such as characterization of complex sample, inference of the main enzymatic pathway involved in a tissue, even to reveal venom composition [ 68 , 69 , 70 , 71 ]. Altogether, 688 peptide sequences were identified among the two replicates of the fractions analyzed (SF and IF), which accounted for 412 groups of non-redundant proteins (), retrieved from custom cnidarians databases.…”

Bibliometric Analysis of Literature in Snake Venom-Related Research Worldwide (1933–2022)

“…Recent focus on snake venom-related research has been gradually shifting to antivenom, proteomics, and transcriptome, providing hints to the emerging subjects in snake venom-related research in the future. In the last few years, there has been an increase in the publication of snake venom proteomes, especially from the families of Elapidae and Viperidae ( Table S3 ) [ 135 , 136 , 137 , 138 , 139 , 140 , 141 , 142 , 143 , 144 , 145 , 146 , 147 , 148 , 149 , 150 , 151 , 152 , 153 , 154 , 155 , 156 , 157 , 158 , 159 , 160 , 161 , 162 , 163 , 164 , 165 , 166 , 167 , 168 , 169 , 170 , 171 , 172 , 173 , 174 , 175 , 176 , 177 , 178 , 179 , 180 , 181 , 182 , 183 , 184 , 1...…”