@article{Wang2026, 
author = {Kailu Wang and Rongfeng Li and Yuzhen Ma and Song Liu and Ronge Xing and Pengcheng Li and Huahua Yu},
title = {Multi-Domain Truncation Strategy Enables Soluble Expression and Analyzing Enzymatic Activity of Nemopilema nomurai Phospholipase A2 Toxin},
year = {2026},
journal = {Periodical of Ocean University of China},
volume = {56},
number = {3},
pages = {91-100},
keywords = {phospholipase A2, protein expression, domain truncation, jellyfish toxin, Nemopilema nomurai},
url = {https://www.sciopen.com/article/10.16441/j.cnki.hdxb.20250127},
doi = {10.16441/j.cnki.hdxb.20250127},
abstract = {As one of the most hazardous jellyfish species in East Asian waters, Nemopilema nomurai is considered a key toxic component that triggers systemic toxicity reactions due to the high abundance of phospholipase A2 (PLA2) isoenzymes in its toxins. This study is based on a transcriptome database and identified four novel venom proteins with typical PLA2 catalytic domains through sequence alignment and three-dimensional structural simulation. By constructing heterologous expression systems of pET-22b and pET-32a, it was found that the full-length recombinant protein presented as inclusion bodies in the E. coli BL21 (DE3) system. To obtain soluble phospholipase A2, we innovatively adopted a multi domain truncation strategy and successfully constructed a truncated PLA2-3 soluble expression system (pET-22b-PLA2-3/BL21 (DE3)). In vitro activity testing confirmed its dose-dependent phospholipid hydrolysis activity. This work establishes for the first time a soluble heterologous expression system of Nemopilema nomurai PLA2 toxin, laying the foundation for further elucidating its toxic molecular mechanism and developing specific detoxifiers.}
}