Selecting key toxins for focused development of elapid snake antivenoms and inhibitors guided by a Toxicity Score

Abstract

For more than 100 years, antivenoms have been produced by traditional methods of immunization of large mammals with mixtures of snake venoms (World Health Organization, 2010 and Gutiérrez et al., 2011). With the introduction of proteomic and transcriptomic tools in the molecular analysis of both venoms (venomics) (Calvete, 2014) and antivenoms (antivenomics) (Calvete, 2011 and Calvete et al., 2014), in combination with the toxicological assessment of venoms, a more in-depth understanding of venom composition and antivenom efficacy is being built. As retrieved from current public databases on Elapidae, values for Median Lethal Dose (LD50) are known for 203 toxins, belonging to seven protein sub-families, originating from 40 species (Fig. 1). Furthermore, the number of elapids for which venom-wide proteomics or transcriptomics studies have been reported has now reached 49 out of 355 described species (our unpublished data; http://www.reptile-database.org). Information is now available for a considerable number of species of high medical relevance.