AI Article Synopsis

  • Snake venoms are complex mixtures of proteins and peptides, and studying their genetic makeup can help identify new toxins and understand their evolution.
  • Researchers sequenced 576 expressed sequence tags (ESTs) from the venom gland of the threatened Desert Massasauga rattlesnake, finding a predominance of serine proteinase and metalloproteinase transcripts, which play a key role in blood disruption.
  • The study discovered unique transcripts encoding rare three-finger toxins and a novel fused toxin, suggesting mechanisms like exon shuffling may contribute to the diversity of snake venoms.

Article Abstract

Background: Snake venoms are complex mixtures of pharmacologically active proteins and peptides which belong to a small number of superfamilies. Global cataloguing of the venom transcriptome facilitates the identification of new families of toxins as well as helps in understanding the evolution of venom proteomes.

Results: We have constructed a cDNA library of the venom gland of a threatened rattlesnake (a pitviper), Sistrurus catenatus edwardsii (Desert Massasauga), and sequenced 576 ESTs. Our results demonstrate a high abundance of serine proteinase and metalloproteinase transcripts, indicating that the disruption of hemostasis is a principle mechanism of action of the venom. In addition to the transcripts encoding common venom proteins, we detected two varieties of low abundance unique transcripts in the library; these encode for three-finger toxins and a novel toxin possibly generated from the fusion of two genes. We also observed polyadenylated ribosomal RNAs in the venom gland library, an interesting preliminary obsevation of this unusual phenomenon in a reptilian system.

Conclusion: The three-finger toxins are characteristic of most elapid venoms but are rare in viperid venoms. We detected several ESTs encoding this group of toxins in this study. We also observed the presence of a transcript encoding a fused protein of two well-characterized toxins (Kunitz/BPTI and Waprins), and this is the first report of this kind of fusion in a snake toxin transcriptome. We propose that these new venom proteins may have ancillary functions for envenomation. The presence of a fused toxin indicates that in addition to gene duplication and accelerated evolution, exon shuffling or transcriptional splicing may also contribute to generating the diversity of toxins and toxin isoforms observed among snake venoms. The detection of low abundance toxins, as observed in this and other studies, indicates a greater compositional similarity of venoms (though potency will differ) among advanced snakes than has been previously recognized.

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2242803PMC
http://dx.doi.org/10.1186/1471-2199-8-115DOI Listing

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