Abstract

The giant jellyfish, Nemopilema nomurai, is widely distributed from the Eastern China Sea to the northern part of the Yellow Sea and has resulted in numerous hospitalizations in coastal areas of China, especially in Northern China. Our previous studies have revealed sting-related proteins in the venom of the jellyfish N. nomurai by using experimental and omics-based approaches; however, the variable symptoms of patients who have been stung by N. nomurai are not fully understood. This limited knowledge led to an examination of whether intraspecific variations occur in the venom of different N. nomurai. In the present study, 13 specimens of N. nomurai were collected from the Yellow Sea, and their venom was characterized by profiling differences in biochemical properties and biological activities. SDS-PAGE analysis presented recognizable differences in the number, intensity and presence of some protein bands. Moreover, enzymatic assays revealed considerable quantitative variations in metalloproteinase activity and PLA2-like activity. In particular, zymography assays of proteases demonstrated the general presence of abundant metalloproteinases in jellyfish nematocyst venom; however, the catalytic activities varied greatly among some specific metalloproteinases in the 28–46 kDa or 57–83 kDa range. Hemolytic assays using sheep erythrocytes suggested a predominant variance in the toxicities of different individual jellyfish venoms, with the difference between the most hemolytic and the least hemolytic venom as large as 77-fold. The current data suggested remarkable variations in the nematocyst venoms of individual N. nomurai jellyfish. These observations will provide a new understanding of the clinical manifestations induced by N. nomurai jellyfish stings and will therefore have important implications for preventing and treating jellyfish envenomations.

Highlights

  • In recent decades, venomous scyphozoans have become increasingly well known for their formidable stinging ability in Eastern Asian waters

  • Previous studies have demonstrated that nematocyst venoms from mature C. barnesi were distinct from those extracted from immature individuals, indicating the occurrence of ontogenetic differences in venom composition[24]

  • These results indicated that the nematocyst venoms from individual jellyfish varied significantly in their nitro-3-octanoyloxybenzoic acid (NOBA)-degrading www.nature.com/scientificreports activities, and the highest phospholipase A2s (PLA2s)-like activity detected in the venoms from J6 and J10 with velocity values of 7.61 ± 0.52 nM/min and 7.60 ± 0.24 nM/min, respectively

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Summary

Introduction

Venomous scyphozoans have become increasingly well known for their formidable stinging ability in Eastern Asian waters. Our previous studies indicated that various enzymatic components, including metalloproteinases and phospholipase A2s (PLA2s), exist in nematocyst venom extracts[6,7], as well as in the proteome of the N. nomurai jellyfish[8]. Www.nature.com/scientificreports may depend on various conditions, such as jellyfish size, area of envenomed skin, and physiological uniqueness. Whether this discrepancy results from variations in venom compositions, such as in the enzymatic constituents, remains unknown for most Scyphozoan jellyfish stings. Previous studies have demonstrated that nematocyst venoms from mature C. barnesi were distinct from those extracted from immature individuals, indicating the occurrence of ontogenetic differences in venom composition[24]. The aim of this study was to provide the first insights into the venom variability in biochemical components and biological activities among different Scyphozoan N. nomurai jellyfish individuals

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