Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom

Venom Proteome of Spine-Bellied Sea Snake (Hydrophis curtus) from Penang, Malaysia: Toxicity Correlation, Immunoprofiling and Cross-Neutralization by Sea Snake Antivenom

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The venom proteome of Hydrophis curtus (synonym: Lapemis hardwickii) from Penang, Malaysia was investigated with nano-electrospray ionization-liquid chromatography tandem mass spectrometry (ESI-LCMS/MS) of the reverse-phase high-performance liquid chromatography (HPLC) venom fractions.Thirty distinct protein forms were identified as toxins from ten families.The three major protein families were phospholipase A2 (PLA2, 62.

0% of total venom proteins), three-finger toxin (3FTX, 26.33%) and cysteine-rich secretory protein (CRiSP, 9.00%).

PLA2 comprises diverse homologues (11 forms), predominantly the acidic subtypes (48.26%).3FTX composed of one short alpha-neurotoxin LIQUID MAKEUP ALMOND BEIGE #1020 (SNTX, 22.

89%) and four long alpha-neurotoxins (LNTX, 3.44%).Both SNTX and LNTX were lethal in mice (intravenous LD50 = 0.

10 and 0.24 μg/g, respectively) but the PLA2 were non-lethal (LD50 >1 μg/g).The more abundant and toxic SNTX appeared to be the main driver of venom lethality (holovenom LD50 = 0.

20 μg/g).The heterologous Sea Snake Antivenom (SSAV, Australia) effectively cross-neutralized the venom (normalized potency = 9.35 mg venom neutralized per g antivenom) and the two neurotoxins Tweed Culottes in vivo, with the LNTX being neutralized more effectively (normalized potency = 3.

5 mg toxin/g antivenom) than SNTX (normalized potency = 1.57 mg/g).SSAV immunorecognition was strong toward PLA2 but moderate-to-weak toward the alpha-neurotoxins, indicating that neutralization of the alpha-neurotoxins should be further improved.