Extensive Variation in the Activities of <i>Pseudocerastes</i> and <i>Eristicophis</i> Viper Venoms Suggests Divergent Envenoming Strategies are Used for Prey Capture

• Main Authors: Bianca op den Brouw, Francisco C. P. Coimbra, Lachlan A. Bourke, Tam Minh Huynh, Danielle H. W. Vlecken, Parviz Ghezellou, Jeroen C. Visser, James S. Dobson, Manuel A. Fernandez-Rojo, Maria P. Ikonomopoulou, Nicholas R. Casewell, Syed Ali, Behzad Fathinia, Wayne C. Hodgson, Bryan G. Fry
• Format: Article
• Language: English
• Published: MDPI AG 2021-02-01
• Series: Toxins
• Subjects: <i>Pseudocerastes</i>; <i>Eristicophis</i>; venom; haemotoxic; neurotoxic; cytotoxic
• Online Access: https://www.mdpi.com/2072-6651/13/2/112

Snakes of the genera <i>Pseudocerastes</i> and <i>Eristicophis</i> (Viperidae: Viperinae) are known as the desert vipers due to their association with the arid environments of the Middle East. These species have received limited research attention and little is known about their venom or ecology. In this study, a comprehensive analysis of desert viper venoms was conducted by visualising the venom proteomes via gel electrophoresis and assessing the crude venoms for their cytotoxic, haemotoxic, and neurotoxic properties. Plasmas sourced from human, toad, and chicken were used as models to assess possible prey-linked venom activity. The venoms demonstrated substantial divergence in composition and bioactivity across all experiments. <i>Pseudocerastes urarachnoides </i>venom activated human coagulation factors X and prothrombin and demonstrated potent procoagulant activity in human, toad, and chicken plasmas, in stark contrast to the potent neurotoxic venom of <i>P. fieldi</i>. The venom of <i>E. macmahonii</i> also induced coagulation, though this did not appear to be via the activation of factor X or prothrombin. The coagulant properties of <i>P. fieldi</i> and <i>P. persicus</i> venoms varied among plasmas, demonstrating strong anticoagulant activity in the amphibian and human plasmas but no significant effect in that of bird. This is conjectured to reflect prey-specific toxin activity, though further ecological studies are required to confirm any dietary associations. This study reinforces the notion that phylogenetic relatedness of snakes cannot readily predict venom protein composition or function. The significant venom variation between these species raises serious concerns regarding antivenom paraspecificity. Future assessment of antivenom is crucial.