A Neurotoxic Snake Venom without Phospholipase A: Proteomics and Cross-Neutralization of the Venom from Senegalese Cobra, (Subgenus: ).

The Senegalese cobra, , is a non-spitting cobra species newly erected from the complex. causes neurotoxic envenomation in Western Africa but its venom properties remain underexplored. Applying a protein decomplexation proteomic approach, this study unveiled the unique complexity of the venom composition. Three-finger toxins constituted the major component, accounting for 75.91% of total venom proteins. Of these, cardiotoxin/cytotoxin (53%) and alpha-neurotoxins (23%) predominated in the venom proteome. Phospholipase A, however, was not present in the venom, suggesting a unique snake venom phenotype found in this species. The venom, despite the absence of PLA, is highly lethal with an intravenous LD of 0.39 µg/g in mice, consistent with the high abundance of alpha-neurotoxins (predominating long neurotoxins) in the venom. The hetero-specific VINS African Polyvalent Antivenom (VAPAV) was immunoreactive to the venom, implying conserved protein antigenicity in the venoms of and . Furthermore, VAPAV was able to cross-neutralize the lethal effect of venom but the potency was limited (0.59 mg venom completely neutralized per mL antivenom, or ~82 LD per ml of antivenom). The efficacy of antivenom should be further improved to optimize the treatment of cobra bite envenomation in Africa.