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Updated: Jul 17, 2026

High Throughput Quantitative Expression Screening and Purification Applied to Recombinant Disulfide-rich Venom Proteins Produced in E. coli
Published on: July 30, 2014
A review on snake venom extracellular vesicles: Past to present
Nagendra K1, Shankar M Bakkannavar2, Vinutha R Bhat3
1Research Scholar, Department of Forensic Medicine and Toxicology, Kasturba Medical College, Manipal, Manipal Academy of Higher Education, Manipal, 576104, India.
Abstract:
Around 95% of snake venom is protein. Along with the soluble proteins, snake venom also contains proteins encapsulated in vesicles known as Snake Venom Extracellular Vesicles (SVEV). SVEVs are nano-sized membrane-bound vesicles released from the snake venom gland cells. The available published research works on SVEVs are minimal. Extracellular vesicles in the Snake Venom gland were initially discovered during the histopathological analysis of the Crotalus durissus terrificus snakes' venom gland. Later, various techniques were employed to isolate and characterize the SVEVs. The cargo of SVEV consists of a variety of proteins like Phospholipase A-2, C-type Lectins, L-Amino Acid Oxidase, Cysteine-Rich Secretory Proteins, Serine Proteinases, Dipeptidyl Peptidase-IV, Aminopeptidase-A, Ecto-5'-nucleotidases, Disintegrins. Proteomic data revealed the presence of some exclusive proteins in the SVEVs, and the other proteins are in varying concentrations in the SVEVs compared to their whole Venom. Interaction of SVEVs with mammalian cell lines showed the disruption of primary physiological functions leads to host immune modulation, and long-term effects of envenoming. Snakebite victim's blood showed variations in the specific Extracellular vesicle concentration. It has been hypothesized that SVEVs are responsible for long-term toxicity. The current review focuses on the various techniques adopted to isolate and characterize SVEVs and discusses the exclusiveness and variations of SVEV proteins and their role in snakebites.
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