Structural characteristics of Heparan sulfate required for the binding with the virus processing Enzyme Furin
文献类型：期刊论文
| 作者 | Zeng, Jiaxin1,2,3; Meng, Yuan3; Chen, Shi-Yi1,3,4; Zhao, Gaofeng1,3; Wang, Lianchun5; Zhang, En-Xin2; Qiu, Hong1,3,4 |
| 刊名 | GLYCOCONJUGATE JOURNAL
 |
| 出版日期 | 2021-10-26 |
| 页码 | 11 |
| 关键词 | Furin Heparan sulfate Heparin Virus infection Carbohydrate-protein interaction |
| ISSN号 | 0282-0080 |
| DOI | 10.1007/s10719-021-10018-8 |
| 通讯作者 | Zhang, En-Xin(ergep53@126.com) ; Qiu, Hong(hongqiu@simm.ac.cn) |
| 英文摘要 | Furin is one of the nine-member proprotein convertase family. Furin cleaves proteins with polybasic residues, which includes many viral glycoproteins such as SARS-Cov-2 spike protein. The cleavage is required for the activation of the proteins. Currently, the mechanisms that regulate Furin activity remain largely unknown. Here we demonstrated that Furin is a novel heparin/heparan sulfate binding protein by the use of biochemical and genetic assays. The K-D is 9.78 nM based on the biolayer interferometry assay. Moreover, we found that sulfation degree, site-specific sulfation (N-sulfation and 3-O-sulfation), and iduronic acid are the major structural determinants for the binding. Furthermore, we found that heparin inhibits the enzymatic activity of Furin when pre-mixes heparin with either Furin or Furin substrate. We also found that the Furin binds with cells of different origin and the binding with the cells of lung origin is the strongest one. These data could advance our understanding of the working mechanism of Furin and will benefit the Furin based drug discovery such as inhibitors targeting the interaction between heparan sulfate and Furin for inhibition of viral infection. |
| WOS关键词 | ACTIVATION ; CLEAVAGE |
| 资助项目 | CAS Pioneer Talent Program in Chinese Academy of Sciences ; Shanghai Pujiang Program[19PJ1411300] |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000711298400001 |
| 出版者 | SPRINGER |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/298332]  |
| 专题 | 中国科学院上海药物研究所 |
| 通讯作者 | Zhang, En-Xin; Qiu, Hong |
| 作者单位 | 1.Univ Chinese Acad Sci, Sch Pharm, 19A Yuquan Rd, Beijing 100049, Peoples R China 2.Guangzhou Univ Chinese Med, Affiliated Hosp 1, 16 Jichang Rd, Guangzhou 510405, Guangdong, Peoples R China 3.Chinese Acad Sci, Carbohydrate Based Drug Res Ctr, Shanghai Inst Mat Med, 555 Zuchongzhi Rd, Shanghai 200031, Peoples R China 4.Nanjing Univ Chinese Med, 138 Xianlin Rd, Nanjing 210023, Peoples R China 5.Univ South Florida Hlth, Morsani Coll Med, Dept Mol Pharmacol & Physiol, Tampa, FL USA |
| 推荐引用方式 GB/T 7714 | Zeng, Jiaxin,Meng, Yuan,Chen, Shi-Yi,et al. Structural characteristics of Heparan sulfate required for the binding with the virus processing Enzyme Furin[J]. GLYCOCONJUGATE JOURNAL,2021:11. |
| APA | Zeng, Jiaxin.,Meng, Yuan.,Chen, Shi-Yi.,Zhao, Gaofeng.,Wang, Lianchun.,...&Qiu, Hong.(2021).Structural characteristics of Heparan sulfate required for the binding with the virus processing Enzyme Furin.GLYCOCONJUGATE JOURNAL,11. |
| MLA | Zeng, Jiaxin,et al."Structural characteristics of Heparan sulfate required for the binding with the virus processing Enzyme Furin".GLYCOCONJUGATE JOURNAL (2021):11. |
入库方式： OAI收割
来源：上海药物研究所
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