Add time:08/02/2019         Source:sciencedirect.com

The venom proteome of Laticauda colubrina (Bali, Indonesia) was elucidated by nano-ESI-LCMS/MS of the venom reverse-phase HPLC fractions. Altogether 31 distinct forms of proteins were identified and clustered into three toxin families: three-finger toxin (3FTX, 66.12% of total venom proteins), phospholipase A2 (PLA2, 33.26%) and cysteine-rich secretory protein (CRiSP, 0.05%). The 3FTX were α-neurotoxins (five long neurotoxins, LNTX, 48.87%; two short neurotoxins, SNTX, 16.94%) and a trace amount of two cytotoxins (CTX, 0.31%). PLA2 were present with a large diversity of homologues (≥ 20 forms), however none was annotated to the lethal proteoform reported previously. The venom is highly lethal in mice (LD50 = 0.10 μg/g) and this is driven primarily by the SNTX and LNTX (LD50 = 0.05–0.13 μg/g), since the PLA2 proteins were non-lethal up to 2 μg/g (20-time the venom LD50). The SNTX and LNTX were effectively cross-neutralized by the heterologous Sea Snake Antivenom (SSAV, Australian product) (potency = 0.27 mg toxin per ml antivenom, and 0.40 mg/ml, respectively), corroborating the cross-neutralization of the whole venom (potency = 1.09 mg/ml) and its antigenic immunoreactivity toward SSAV. Furthermore, compared with earlier studies, the present work reveals geographical variation of venom composition for L. colubrina which may have implication for the evolution and conservation of the species.

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