中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Discovery of a novel jellyfish venom metalloproteinase inhibitor from secondary metabolites isolated from jellyfish-derived fungus Aspergillus versicolor SmT07

文献类型:期刊论文

作者Yue, Yang1,3; Yu, Huahua1,2; Suo, Qishan1,3,4; Li, Rongfeng1,2; Liu, Song1,2; Xing, Ronge1,2; Zhang, Quanbin1,3; Li, Pengcheng1,2
刊名CHEMICO-BIOLOGICAL INTERACTIONS
出版日期2022-09-25
卷号365页码:8
ISSN号0009-2797
关键词Nemopilema nomurai Jellyfish envenomations Aspergillus versicolor Metalloproteinase inhibitors Molecular docking
DOI10.1016/j.cbi.2022.110113
通讯作者Yu, Huahua(yuhuahua@qdio.ac.cn)
英文摘要The major jellyfish stings that occur in China are caused by scyphozoan Nemopilema nomurai, whose venom exhibits significant metalloproteinase activity that contributes to the toxic effects of jellyfish envenomation. Researching effective inhibitors suppressing the metalloproteinase activity of jellyfish venom represents a new attempt to cure jellyfish envenomations. In the present study, secondary metabolites produced by the jellyfishassociated fungus Aspergillus versicolor SmT07 were isolated and evaluated for their anti-proteolytic activities. Two xanthones, sterigmatocystin (JC-01) and oxisterigmatocystin C (JC-06), and four alkaloids, cottoquinazoline A (JC-02), phenazine-1-carboxylic acid (JC-03), viridicatin (JC-04) and viridicatol (JC-05), were isolated and identified. Only phenazine-1-carboxylic acid (PCA) showed significant anti-proteolytic activity of jellyfish venom assayed on azocasein, and the IC50 value was 2.16 mM. PCA also significantly inhibited fibrinogenolytic activity, protecting the B beta chain of fibrinogen from degradation when preincubated with jellyfish venom at a ratio of >1:0.6 (PCA:venom, w/w). Molecular docking with several well-characterized snake venom metalloproteinases suggested the venom metalloproteinases inhibitory property of PCA by forming complex interactions with the active site via hydrogen bonds, 7C-7C stacking and salt bridges, which was distinct from the binding mode of batimastat. The present study represents the first study identifying natural jellyfish venom metalloproteinase inhibitors from marine natural products, which may provide an alternative to develop therapeutic agents for treating jellyfish envenomations.
资助项目National Natural Science Foundation of China[41906082] ; Natural Science Foundation of Shandong Province[ZR2019BD025] ; Natural Science Foundation of Shandong Province[ZR2019QD012] ; National Key R & D Program of China[2017YFE0111100-04] ; National Key R & D Program of China[2019YFC0312605] ; Major Projects on the Transformation of Old and Novel Kinetic Energy of Shandong Province[2020-1220]
WOS研究方向Biochemistry & Molecular Biology ; Pharmacology & Pharmacy ; Toxicology
语种英语
出版者ELSEVIER IRELAND LTD
WOS记录号WOS:000874830700005
源URL[http://ir.qdio.ac.cn/handle/337002/180557]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Yu, Huahua
作者单位1.Chinese Acad Sci, Inst Oceanol, Ctr Ocean Mega Sci, CAS & Shandong Prov Key Lab Expt Marine Biol, 7 Nanhai Rd, Qingdao 266071, Peoples R China
2.Pilot Qingdao Natl Lab Marine Sci & Technol, Lab Marine Drugs & Bioprod, 1 Wenhai Rd, Qingdao 266237, Peoples R China
3.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China
4.Univ Chinese Acad Sci, Beijing, Peoples R China
推荐引用方式
GB/T 7714
Yue, Yang,Yu, Huahua,Suo, Qishan,et al. Discovery of a novel jellyfish venom metalloproteinase inhibitor from secondary metabolites isolated from jellyfish-derived fungus Aspergillus versicolor SmT07[J]. CHEMICO-BIOLOGICAL INTERACTIONS,2022,365:8.
APA Yue, Yang.,Yu, Huahua.,Suo, Qishan.,Li, Rongfeng.,Liu, Song.,...&Li, Pengcheng.(2022).Discovery of a novel jellyfish venom metalloproteinase inhibitor from secondary metabolites isolated from jellyfish-derived fungus Aspergillus versicolor SmT07.CHEMICO-BIOLOGICAL INTERACTIONS,365,8.
MLA Yue, Yang,et al."Discovery of a novel jellyfish venom metalloproteinase inhibitor from secondary metabolites isolated from jellyfish-derived fungus Aspergillus versicolor SmT07".CHEMICO-BIOLOGICAL INTERACTIONS 365(2022):8.

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来源:海洋研究所

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