The remarkably enzyme-rich venom of the Big Bend Scorpion (Diplocentrus whitei).

Scorpion venoms have long been studied for their peptide discovery potential, with modern high-throughput venom-characterization techniques paving the way for the discovery of thousands of novel putative toxins. Research into these toxins has provided insight into the pathology and treatment of human diseases, even resulting in the development of one compound with Food and Drug Administration (FDA) approval. Although most of this research has focused on the toxins of scorpion species considered medically significant to humans, the venom of harmless scorpion species possess toxins that are homologous to those from medically significant species, indicating that harmless scorpion venoms may also serve as valuable sources of novel peptide variants. Furthermore, as harmless scorpions represent a vast majority of scorpion species diversity, and therefore venom toxin diversity, venoms from these species likely contain entirely new toxin classes. We sequenced the venom-gland transcriptome and venom proteome of two male Big Bend scorpions (Diplocentrus whitei), providing the first high-throughput venom characterization for a member of this genus. We identified a total of 82 toxins in the venom of D. whitei , 25 of which were identified in both the transcriptome and proteome, and 57 of which were only identified in the transcriptome. Furthermore, we identified a unique, enzyme-rich venom dominated by serine proteases and the first arylsulfatase B toxins identified in scorpions. [Display omitted] • High-throughput venom proteomic and venom-gland transcriptomic characterization of two male Diplocentrus whitei. • Diplocentrus whitei venom displayed a remarkable abundance and diversity of enzymatic venom components. • High abundance of novel arylsulfatase B toxins and serine proteases in Diplocentrus whitei venom. • Identified 25 proteomically confirmed toxins and 57 homology-based toxins in Diplocentrus whitei venom. • Diplocentrus whitei venom proteomic abundances display strong agreement between individuals. [ABSTRACT FROM AUTHOR]