NnM469, a novel recombinant jellyfish venom metalloproteinase from Nemopilema nomurai, disrupted the cell matrix
文献类型：期刊论文
| 作者 | Ma, Yuzhen1; Yu, Huahua2,3,4 ; Teng, Lichao2,3,5; Geng, Hao2,3,5; Li, Rongfeng2,3,4; Xing, Ronge2,3,4; Liu, Song2,3,4; Li, Pengcheng2,3,4
|
| 刊名 | INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
 |
| 出版日期 | 2024-11-01 |
| 卷号 | 281页码:10 |
| 关键词 | Jellyfish venom Dermatitis Metalloproteinase Nemopilema nomurai |
| ISSN号 | 0141-8130 |
| DOI | 10.1016/j.ijbiomac.2024.136531 |
| 通讯作者 | Yu, Huahua(yuhuahua@qdio.ac.cn) |
| 英文摘要 | Molecular cloning and functional characterization of Nemopilema nomurai venom metalloproteinases have provided deeper insights into the pathogenesis of jellyfish dermatitis. This study reports a new cDNA clone from N. nomurai tentacle venom (Transcript sequence: ID469) encoding 362 amino acid residues, belonged to astacin family and capable of disrupting the cell matrix. The N. nomurai metalloproteinase 469 (NnM469) comprises a signal peptide and propeptide, followed by metalloproteinase domain containing a zinc-binding motif, and two ShKT domains. Notably, NnM469 features a zinc-binding motif (HEXXH) at the active site, within an extended sequence of H E XX H XXGFX H E, which is unique to astacin. Immunocytochemistry revealed that NnM469 is located in the stab tube and envelope of jellyfish nematocysts. Western blot and LC-MS/MS analysis confirmed that the NnM469 protein was successfully expressed using the Pichia pastoris expression system. The recombinant NnM469 could degrade the cell matrix, resulting in the death of HaCaT cells with an IC50 of 26.34 mu g/mL. Finally, I-TASSER-generated structure and function predictions indicated that conserved Asp53, His168, His172, His178, and Tyr227 serve as key amino acid residues for the Zn2+ ion binding in the catalytic center. In summary, the study of the molecular characteristics and function of NnM469 presents an opportunity to develop therapeutic interventions for jellyfish venom-induced dermatitis. |
| WOS关键词 | SNAKE-VENOM ; ZINC METALLOPROTEINASE ; PROTEIN ; ASTACIN |
| 资助项目 | National Natural Science Foundation of China[41776163] ; National Natural Science Foundation of China[41876164] ; National Key Research and Development Program of China[2017YFE0111100-04] ; National Key Research and Development Program of China[2019YFC0312605] |
| WOS研究方向 | Biochemistry & Molecular Biology ; Chemistry ; Polymer Science |
| 语种 | 英语 |
| WOS记录号 | WOS:001340024300001 |
| 出版者 | ELSEVIER |
| 源URL | [http://ir.qdio.ac.cn/handle/337002/199561]  |
| 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.Qingdao Univ Sci & Technol, Coll Biol Engn, Qingdao 266042, Shandong, Peoples R China 2.Chinese Acad Sci, Qingdao 266000, Peoples R China 3.Chinese Acad Sci, Inst Oceanol, Shandong Prov Key Lab Expt Marine Biol, Qingdao 266000, Peoples R China 4.Qingdao Marine Sci & Technol Ctr, Lab Marine Drugs & Bioprod, Qingdao 266237, Peoples R China 5.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
| 推荐引用方式 GB/T 7714 | Ma, Yuzhen,Yu, Huahua,Teng, Lichao,et al. NnM469, a novel recombinant jellyfish venom metalloproteinase from Nemopilema nomurai, disrupted the cell matrix[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2024,281:10. |
| APA | Ma, Yuzhen.,Yu, Huahua.,Teng, Lichao.,Geng, Hao.,Li, Rongfeng.,...&Li, Pengcheng.(2024).NnM469, a novel recombinant jellyfish venom metalloproteinase from Nemopilema nomurai, disrupted the cell matrix.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,281,10. |
| MLA | Ma, Yuzhen,et al."NnM469, a novel recombinant jellyfish venom metalloproteinase from Nemopilema nomurai, disrupted the cell matrix".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 281(2024):10. |
入库方式： OAI收割
来源：海洋研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。