Proteome analysis of snake venom toxins: pharmacological insights

Abstract

Snake venoms are an extremely rich source of pharmacologically active proteins with a considerable clinical and medical potential. To date, this potential has not been fully explored, mainly because of our incomplete knowledge of the venom proteome and the pharmacological properties of its components, in particular those devoid of enzymatic activity. This review summarizes the latest achievements in the determination of snake venom proteome, based primarily on the development of new strategies and techniques. Detailed knowledge of the venom toxin composition and biological properties of the protein constituents should provide the scaffold for the design of new more effective drugs for the treatment of the hemostatic system and heart disorders, inflammation, cancer and consequences of snake bites, as well as new tools for clinical diagnostic and assays of hemostatic parameters.

Mapping Proteoforms and Protein Complexes From King Cobra Venom Using Both Denaturing and Native Top-down Proteomics

“…Comparing our BU identifications to recently published papers that used BU for protein identification in O. hannah venom, we were able to identify 80 and 40% more protein families than the identifications presented by Petras et al (21) and Vonk and co-workers (36), respectively. Notable differences may be related to the different methodologies applied, instrumentation used, and/or variation in snake venom sample (4,7,8). Our BU quantitation results showed large amounts of 3FTx in the venom that is consistent with the previous studies of the king cobra venom proteome (21,36,67) and with the rapid neurotoxicity because of muscular transmission blockage (i.e.…”

“…Snake venoms in particular are widely studied and contain a mixture of small molecules, peptides, proteins, and protein complexes which are used to incapacitate prey and to defend against predators (3)(4)(5). Snakes produce anywhere from three to several dozen diverse families of toxic proteins.…”

“…Snakes produce anywhere from three to several dozen diverse families of toxic proteins. Each family is encoded by multiple multilocus genes generated by gene duplication resulting in a large number of expressed isoforms (6) that can differ greatly even between individuals of the same species (4,7,8).…”

Venomics of the beaked sea snake, Hydrophis schistosus: A minimalist toxin arsenal and its cross-neutralization by heterologous antivenoms

“…Our knowledge on the proteomes of venom has advanced remarkably since then, shedding light on the improvement of snakebite management as well as drug discovery [26][27][28][29]. To date, the proteomes of a considerable number of medically important venomous snakes have been reported (for examples: [31][32][33][34][35][36]), however, there were limited studies published on the proteome of sea snake venoms [37][38].…”

Snake venomics of two poorly known Hydrophiinae: Comparative proteomics of the venoms of terrestrial Toxicocalamus longissimus and marine Hydrophis cyanocinctus

“…Research on venoms has been continuously improved by advances in technology. The emergence of "-omic" technologies in the field of toxinology at the turn of the 21st century offered the unprecedented possibility to explore global biological trends and expand our understanding of the clinical correlation of the global toxin composition of venoms [41][42][43][44]. Here we apply snake venomics to unveil and compare the toxin profiles of two Hydrophiinae venoms: that of a basal terrestrial AustraloMelanesian elapid, Toxicocalamus longissimus, and that of a more recently evolved sea snake, Hydrophis cyanocinctus.…”