Characterization and neutralization of Nemopilema nomurai (Scyphozoa: Rhizostomeae) jellyfish venom using polyclonal antibody

• Published in: Toxicon (Oxford) 2014-08, Vol.86, p.116-125
• Main Authors: Kang, Changkeun, Han, Dae-yong, Park, Kwang-Il, Pyo, Min-Jung, Heo, Yunwi, Lee, Hyunkyoung, Kim, Gon Sup, Kim, Euikyung
• Format: Article
• Language: English
• Subjects: Animals; Antibodies; Antibodies, Neutralizing - chemistry; Antivenins - chemistry; Assaying; Cnidarian Venoms - chemistry; Cnidarian Venoms - immunology; Enzyme-Linked Immunosorbent Assay; Enzymes; Jellyfish venom; Mass Spectrometry; Mice; Nemopilema nomurai; Neutralization Tests; Neutralizing; Neutralizing antibody; Protective effect; Proteins; Rabbits; Rhizostomeae; Scyphozoa; Toxicity; Toxicity Tests
• ISSN: 0041-0101; 1879-3150
• DOI: 10.1016/j.toxicon.2014.04.005

Jellyfish stings have often caused serious health concerns for sea bathers especially in tropical waters. In the coastal areas of Korea, China and Japan, the blooming and stinging accidents of poisonous jellyfish species have recently increased, including Nemopilema nomurai. We have generated a polyclonal antibody against N. nomurai jellyfish venom (NnV) by the immunization of white rabbits with NnV antigen. In the present study, the antibody has been characterized for its neutralizing effect against NnV. At first, the presence of NnV polyclonal antibody has been confirmed from the immunized rabbit serum by Enzyme linked immunosorbent assay (ELISA). Then, the neutralizing activities of the polyclonal antibody have been investigated using cell-based toxicity test, hemolysis assay, and mice lethality test. When the polyclonal antibody was preincubated with NnV, it shows a high effectiveness in neutralizing the NnV toxicities in a concentration-dependent manner. Moreover, we explored proteomic analyses using 2-D SDS-PAGE and MALDI-TOF mass spectrometry to illustrate the molecular identities of the jellyfish venom. From this, 18 different protein families have been identified as jellyfish venom-derived proteins; the main findings of which are matrix metalloproteinase-14, astacin-like metalloprotease toxin 3 precursor. It is expected that the present results would have contributed to our understandings of the envenomation by N. nomurai, their treatment and some valuable knowledge on the pathological processes of the jellyfish stinging. •We generate a polyclonal antibody against Nemopilema nomurai jellyfish venom.•We observe the polyclonal antibody is effective in neutralizing jellyfish venom cytotoxicity and hemolytic activity.•The mice lethality of the venom can be suppressed by the antibody premixed with the venom.•The molecular identities of N. nomurai venom were explored using 2-D SDS-PAGE and MALDI-TOF MS.•We suggest a possible intervention of N. nomurai jellyfish envenomation using a specific antibody.