Abstract
Snake venom toxins are responsible for causing severe pathology and toxicity following envenomation including necrosis, apoptosis, neurotoxicity, myotoxicity, cardiotoxicity, profuse hemorrhage, and disruption of blood homeostasis. Clinically, snake venom toxins therefore represent a significant hazard to snakebite victims which underscores the need to produce more efficient anti-venom. Some snake venom toxins, however, have great potential as drugs for treating human diseases. In this review, we discuss the biochemistry, structure/function, and pathology induced by snake venom toxins on human tissue. We provide a broad overview of cobra venom cytotoxins, catalytically active and inactive phospholipase A2s (PLA2s), and Zn2+-dependent metalloproteinases. We also propose biomedical applications whereby snake venom toxins can be employed for treating human diseases. Cobra venom cytotoxins, for example, may be utilized as anti-cancer agents since they are efficient at destroying certain types of cancer cells including leukemia. Additionally, increasing our understanding of the molecular mechanism(s) by which snake venom PLA2s promote hydrolysis of cell membrane phospholipids can give insight into the underlying biomedical implications for treating autoimmune disorders that are caused by dysregulated endogenous PLA2 activity. Lastly, we provide an exhaustive overview of snake venom Zn2+-dependent metalloproteinases and suggest ways by which these enzymes can be engineered for treating deep vein thrombosis and neurodegenerative disorders.
Highlights
Snake venom is a complex mixture of organic compounds [1]
Overall, elucidating the transient structural changes on the molecular organization of phospholipid interfaces induced by phospholipase A2s (PLA2s) in cell membranes should aid the design of basic peptides that suppress overactive endogenous PLA2s as seen in various autoimmune disorders and in chronic inflammatory conditions including rheumatoid arthritis, asthma, and possibly in some neurodegenerative diseases [18]
vascular apoptosis-inducing protein 1 (VAP1) and monomeric VAP2 [148] are weakly hemorrhagic toxins [149], the findings shown by Araki et al 2002 [124] suggest that the disintegrin domain of the P-III snake venom hemorrhagic metalloproteinases (SVMPs) must be at least partly involved for promoting apoptosis
Summary
Snake venom is a complex mixture of organic compounds [1]. Many of these compounds produce a variety of pathophysiological effects including local tissue damage and/or systemic effects in the affected individual [1,2,3,4]. The non-obligatory protein-binding partners of cytotoxins in snake venom are the catalytically active PLA2s.
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