Identification of an antiviral component from the venom of the scorpion Liocheles australasiae using transcriptomic and mass spectrometric analyses

Abstract

Scorpion venom contains a variety of biologically active peptides. Among them, neurotoxins are major components in the venom, but it also contains peptides that show antimicrobial activity. Previously, we identified three insecticidal peptides from the venom of the Liocheles australasiae scorpion, but activities and structures of other venom components remained unknown. In this study, we performed a transcriptome analysis of the venom gland of the scorpion L. australasiae to gain a comprehensive understanding of its venom components. The result shows that potassium channel toxin-like peptides were the most diverse, whereas only a limited number of sodium channel toxin-like peptides were observed. In addition to these neurotoxin-like peptides, many non-disulfide-bridged peptides were identified, suggesting that these components have some critical roles in the L. australasiae venom. In this study, we also isolated a component with antiviral activity against hepatitis C virus using a bioassay-guided fractionation approach. By integrating mass spectrometric and transcriptomic data, we successfully identified LaPLA₂-1 as an anti-HCV component. LaPLA₂-1 is a phospholipase A₂ having a heterodimeric structure that is N-glycosylated at the N-terminal region. Since the antiviral activity of LaPLA₂-1 was inhibited by a PLA₂ inhibitor, the enzymatic activity of LaPLA₂-1 is likely to be involved in its antiviral activity.

Keywords: Bioactive peptide; Glycosylation; Hepatitis C; Phospholipase; Venom gland.