Abstract
BackgroundBecause jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. Although the effects of their toxins are a matter of concern, information on the venom components, biological activity and pathological mechanisms are still scarce. Therefore, the aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics.MethodsTo determine the relationship between fibrinolytic activity of NnV and the serine protease, fibrin zymography was performed using metalloprotease and serine protease inhibitors. The biochemical characterization of serine proteases of NnV were determined by the amidolytic assay. Fractions with fibrinolytic activity were obtained by DEAE cation exchange column.ResultsNnV displayed fibrinolytic activities with molecular masses of approximately 70, 35, 30, and 28 kDa. The fibrinolytic activity of NnV was completely obliterated by phenylmethylsulfonyl fluoride, a prototype serine protease inhibitor. Based on amidolytic assays using chromogenic substrates specific for various kinds of serine proteases, NnV predominantly manifested a chymotrypsin-like feature. Its activity was completely eliminated at low pH (< 6) and high temperatures (> 37 °C). Some metal ions (Co2+, Cu2+, Zn2+ and Ni2+) strongly suppressed its fibrinolytic activity, while others (Ca2+ and Mg2+) failed to do so. Isolation of a serine protease with fibrionolytic activity from NnV revealed that only p3 showed the fibrinolytic activity, which was completely inhibited by PMSF.ConclusionThe present study showed that N. nomurai jellyfish venom has a chymotrypsin-like serine protease with fibrinolytic activity. Such information might be useful for developing clinical management of jellyfish envenomation and pharmacological agents with therapeutic potential for thrombotic diseases in the future.
Highlights
Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms
Nemopilema nomurai jellyfish venom (NnV) was incubated with different pH buffers, including 0.5 M acetate, 0.1 M phosphate and SDS-PAGE and fibrinolytic activity of NnV To compare the fibrinolytic activity between different jellyfish species, their venom proteins were loaded into fibrin zymogrpahy
P. physalis venom was highly potent for fibrin degradation and its molecular weight was above 25 kDa
Summary
Because jellyfish are capable of provoking envenomation in humans, they are considered hazardous organisms. The aim of the present study was to investigate a serine protease component of Nemopilema nomurai jellyfish venom (NnV) and unveil its characteristics. There has been a dramatic increase of global jellyfish blooming from many places in the world, including the oceans of Korea, China, and Japan. Jellyfish blooming can cause a number of social, economic, and public health problems. Power plants may shutdown due to jellyfish clogging the cooling water. Nemopilema nomurai is a giant jellyfish with a bell size up to 2 m in diameter. This jellyfish is one of the dominant jellyfish species in Korean coast.
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