Identification of an antiviral component from the venom of the scorpion Liocheles australasiae using transcriptomic and mass spectrometric analyses. (February 2021)
- Record Type:
- Journal Article
- Title:
- Identification of an antiviral component from the venom of the scorpion Liocheles australasiae using transcriptomic and mass spectrometric analyses. (February 2021)
- Main Title:
- Identification of an antiviral component from the venom of the scorpion Liocheles australasiae using transcriptomic and mass spectrometric analyses
- Authors:
- Miyashita, Masahiro
Mitani, Naoya
Kitanaka, Atsushi
Yakio, Mao
Chen, Ming
Nishimoto, Sachiko
Uchiyama, Hironobu
Sue, Masayuki
Hotta, Hak
Nakagawa, Yoshiaki
Miyagawa, Hisashi - Abstract:
- 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. Graphical abstract: Image 1 Highlights: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. Graphical abstract: Image 1 Highlights: Transcriptome analysis of the venom gland of the scorpion Liocheles australasiae was performed. Among components identified, potassium channel toxin-like peptides were the most diverse. A component with antiviral activity against hepatitis C virus was isolated using a bioassay-guided fractionation approach. Mass spectrometric analysis revealed that this component is one of the PLA2 s with N-glycosylation. … (more)
- Is Part Of:
- Toxicon. Volume 191(2021)
- Journal:
- Toxicon
- Issue:
- Volume 191(2021)
- Issue Display:
- Volume 191, Issue 2021 (2021)
- Year:
- 2021
- Volume:
- 191
- Issue:
- 2021
- Issue Sort Value:
- 2021-0191-2021-0000
- Page Start:
- 25
- Page End:
- 37
- Publication Date:
- 2021-02
- Subjects:
- Bioactive peptide -- Glycosylation -- Hepatitis C -- Phospholipase -- Venom gland
Toxins -- Periodicals
Venom -- Periodicals
615.9 - Journal URLs:
- http://www.sciencedirect.com/science/journal/00410101 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.toxicon.2020.12.007 ↗
- Languages:
- English
- ISSNs:
- 0041-0101
- Deposit Type:
- Legaldeposit
- View Content:
- Available online (eLD content is only available in our Reading Rooms) ↗
- Physical Locations:
- British Library DSC - 8873.050000
British Library DSC - BLDSS-3PM
British Library HMNTS - ELD Digital store - Ingest File:
- 15544.xml