Abstract
The use of -omics technologies allows for the characterization of snake venom composition at a fast rate and at high levels of detail. In the present study, we investigated the protein content of Red-headed Krait (Bungarus flaviceps) venom. This analysis revealed a high diversity of snake venom protein families, as evidenced by high-throughput mass spectrometric analysis. We found all six venom protein families previously reported in a transcriptome study of the venom gland of B. flaviceps, including phospholipases A2 (PLA2s), Kunitz-type serine proteinase inhibitors (KSPIs), three-finger toxins (3FTxs), cysteine-rich secretory proteins (CRISPs), snaclecs, and natriuretic peptides. A combined approach of automated database searches and de novo sequencing of tandem mass spectra, followed by sequence similarity searches, revealed the presence of 12 additional toxin families. De novo sequencing alone was able to identify 58 additional peptides, and this approach contributed significantly to the comprehensive description of the venom. Abundant protein families comprise 3FTxs (22.3%), KSPIs (19%), acetylcholinesterases (12.6%), PLA2s (11.9%), venom endothelial growth factors (VEGFs, 8.4%), nucleotidases (4.3%), and C-type lectin-like proteins (snaclecs, 3.3%); an additional 11 toxin families are present at significantly lower concentrations, including complement depleting factors, a family not previously detected in Bungarus venoms. The utility of a multifaceted approach toward unraveling the proteome of snake venoms, employed here, allowed detection of even minor venom components. This more in-depth knowledge of the composition of B. flaviceps venom facilitates a better understanding of snake venom molecular evolution, in turn contributing to more effective treatment of krait bites.
Highlights
In the last decade, there has been a tremendous increase in the knowledge of snake venom composition and evolution, mainly because of the application of “omics” techniques, in particular, high-throughput transcriptomic investigations of venom gland tissue in combination with proteomic studies of venom [1,2,3,4,5,6]
The venom proteome of the elapid B. flaviceps was investigated by mass spectrometric analysis
The venom proteome of the elapid B. flaviceps was investigated by mass spectrometric analysis of database searches and BLAST analyses of de novo sequenced tandem mass spectra, we were using complementary ionization techniques, including electrospray and MALDI
Summary
There has been a tremendous increase in the knowledge of snake venom composition and evolution, mainly because of the application of “omics” techniques, in particular, high-throughput transcriptomic investigations of venom gland tissue in combination with proteomic studies of venom [1,2,3,4,5,6]. The authors reasoned that this is the first example in which a contrasting pattern of toxicity in relation to diet has been shown for proteins in the venom of a single snake As these technologies are applied to poorly known venoms, new toxins may be discovered, as demonstrated by an investigation of the proteome and transcriptome of the venom of the Australian elapid snake Drysdalia coronoides, which revealed, among other protein families, novel three-finger toxins (3FTx) proteins [10]. Brown Treesnake (Boiga irregularis), and Green Vinesnake (Oxybelis fulgidus), two rear-fanged colubrid snakes, both feed primarily on lizards and birds, and their venoms contain different novel 3FTxs that are specific for these taxa and are harmless toward mammals [11,12], strongly indicating selection for taxon-specific venom toxins These examples point to the significance of deep mining venomics studies by, for example, combined transcriptome and proteome investigations to detect even less abundant venom sequences that might be of biological or pharmaceutical importance. We investigated the venom proteome of B. flaviceps by a complementary approach of electrospray and MALDI mass spectrometry (MS) to probe deeply for even minor venom compounds
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