Citation

K N, Bakkannavar SM, Bhat VR, Sirur FM. Toxicon 2024; ePub(ePub): ePub.

Copyright

(Copyright © 2024, Elsevier Publishing)

DOI

10.1016/j.toxicon.2024.107772

PMID

38768828

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.

Language: en

Keywords

Snake Venom; Snake Venom Extracellular Vesicles; Snake Venom toxins; Snakebite burden; Venomics