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://dx.doi.org/10.1186/1471-2199-8-115 | DOI Listing |
Trans R Soc Trop Med Hyg
January 2025
Department of Radiodiagnosis, Dr RPGMC, Tanda, Kangra (HP) India 176001.
We describe a series of five patients with bilateral parotid enlargement as a sequalae to envenomation by the common krait (Bungarus caeruleus). Fine-needle aspiration cytology of the parotid gland was performed in four cases. The cytology revealed a mild lymphocytic inflammatory response in a red blood cell mixed proteinaceous background.
View Article and Find Full Text PDFToxins (Basel)
November 2024
Facultad de Ciencias Exactas y Naturales, Pontificia Universidad Católica del Ecuador, Quito 170525, Ecuador.
Previous proteomic studies of viperid venom revealed that it is mainly composed of metalloproteinases (SVMPs), serine proteinases (SVSPs), phospholipase A2 (PLA2), and C-type lectins (CTLs). However, other proteins appear in minor amounts that affect prey and need to be identified. This study aimed to identify novel toxic proteins in the venom gland transcriptome of and , using data from NCBI.
View Article and Find Full Text PDFJ Fungi (Basel)
December 2024
Division of Pharmacognosy and Toxicology, Faculty of Pharmaceutical Sciences, Khon Kaen University, Khon Kaen 40002, Thailand.
Hyaluronidases have been a subject of great interest in medical and cosmeceutical applications. Previously, our group demonstrated that the venom glands of contain hyaluronidase enzymes (VesT2s), and heterologous expression of the corresponding gene () in systems results in inclusion bodies, necessitating functional folding using urea. Here, we report the successful heterologous expression of VesT2a in the expression system, with gene construction achieved using Golden.
View Article and Find Full Text PDFMicrob Ecol
December 2024
Hebei Basic Science Center for Biotic Interaction, Hebei University, Baoding, 071002, Hebei, China.
Spiders are natural predators of agricultural pests, primarily due to the potent venom in their venom glands. Spider venom is compositionally complex and holds research value. This study analyzes the diversity of symbiotic bacteria in spider venom glands and venom, as well as the biological activity of culturable symbiotic bacteria.
View Article and Find Full Text PDFToxicon
December 2024
Departamento de Farmacologia, Faculdade de Ciências Médicas, Universidade Estadual de Campinas (UNICAMP), Rua Vital Brazil, 80, Cidade Universitária Zeferino Vaz, 13083-888, Campinas, SP, Brazil. Electronic address:
The venom of Colombian specimens of the rear-fanged snake Pseudoboa neuwiedii contains proteolytic and phospholipase A (PLA) activities, but is devoid of esterases. Mass spectrometric analysis of electrophoretic bands indicated that this venom contains C-type lectins (CTL), cysteine-rich secretory proteins (CRiSP), PLA, snake venom metalloproteinases (SVMP), and snake venom matrix metalloproteinases (svMMP). In this investigation, we extended our characterization of P.
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