Jellyfish venomics and venom gland transcriptomics analysis of Stomolophus meleagris to reveal the toxins associated with sting

J Proteomics. 2014 Jun 25:106:17-29. doi: 10.1016/j.jprot.2014.04.011. Epub 2014 Apr 18.

Abstract

Jellyfish Stomolophus meleagris is a very dangerous animal because of its strong toxicity. However, the composition of the venom is still unclear. Both proteomics and transcriptomics approaches were applied in present study to investigate the major components and their possible relationships to the sting. The proteomics of the venom from S. meleagris was conducted by tryptic digestion of the crude venom followed by RP-HPLC separation and MS/MS analysis of the tryptic peptides. The venom gland transcriptome was analyzed using a high-throughput Illumina sequencing platform HiSeq 2000 with de novo assembly. A total of 218 toxins were identified including C-type lectin, phospholipase A₂ (PLA₂), potassium channel inhibitor, protease inhibitor, metalloprotease, hemolysin and other toxins, most of which should be responsible for the sting. Among them, serine protease inhibitor, PLA₂, potassium channel inhibitor and metalloprotease are predominant, representing 28.44%, 21.56%, 16.06% and 15.14% of the identified venom proteins, respectively. Overall, our combined proteomics and transcriptomics approach provides a systematic overview of the toxins in the venom of jellyfish S. meleagris and it will be significant to understand the mechanism of the sting.

Biological significance: Jellyfish Stomolophus meleagris is a very dangerous animal because of its strong toxicity. It often bloomed in the coast of China in recent years and caused thousands of people stung and even deaths every year. However, the components which caused sting are still unknown yet. In addition, no study about the venomics of jellyfish S. meleagris has been reported. In the present study, both proteomics and transcriptomics approaches were applied to investigate the major components related to the sting. The result showed that major component included C-type lectin, phospholipase A₂, potassium channel inhibitor, protease inhibitor, metalloprotease, hemolysin and other toxins, which should be responsible for the effect of sting. This is the first research about the venomics of jellyfish S. meleagris. It will be significant to understand the mechanism of the biological effects and helpful to develop ways to deal with the sting.

Keywords: Jellyfish; Sting; Stomolophus meleagris; Toxin; Transcriptomics; Venomics.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • China
  • Chromatography, High Pressure Liquid
  • Computational Biology
  • Gene Library
  • Geography
  • Lectins / chemistry
  • Mass Spectrometry
  • Molecular Sequence Data
  • Phospholipases A2 / chemistry
  • Potassium Channels / chemistry
  • Protein Structure, Tertiary
  • Proteome
  • Proteomics / methods
  • Scyphozoa / chemistry*
  • Sequence Analysis, DNA
  • Sequence Homology, Amino Acid
  • Tandem Mass Spectrometry
  • Transcriptome*
  • Trypsin
  • Venoms / chemistry*

Substances

  • Lectins
  • Potassium Channels
  • Proteome
  • Venoms
  • Phospholipases A2
  • Trypsin