Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
文献类型：期刊论文
| 作者 | Lu, Guangwen1; Hu, Yawei2; Wang, Qihui1; Qi, Jianxun1; Gao, Feng3,4; Li, Yan1; Zhang, Yanfang1,5; Zhang, Wei1; Yuan, Yuan1,6; Bao, Jinku4 |
| 刊名 | NATURE
 |
| 出版日期 | 2013-08-08 |
| 卷号 | 500期号:7461页码:227-+ |
| 英文摘要 | The newly emergent Middle East respiratory syndrome coronavirus (MERS-CoV) can cause severe pulmonary disease in humans(1,2), representing the second example of a highly pathogenic coronavirus, the first being SARS-CoV3. CD26 (also known as dipeptidyl peptidase 4, DPP4) was recently identified as the cellular receptor for MERS-CoV4. The engagement of the MERS-CoV spike protein with CD26 mediates viral attachment to host cells and virus-cell fusion, thereby initiating infection. Here we delineate the molecular basis of this specific interaction by presenting the first crystal structures of both the free receptor binding domain (RBD) of the MERS-CoV spike protein and its complex with CD26. Furthermore, binding between the RBD and CD26 is measured using real-time surface plasmon resonance with a dissociation constant of 16.7 nM. The viral RBD is composed of a core subdomain homologous to that of the SARS-CoV spike protein, and a unique strand-dominated external receptor binding motif that recognizes blades IV and V of the CD26 beta-propeller. The atomic details at the interface between the two binding entities reveal a surprising protein-protein contact mediated mainly by hydrophilic residues. Sequence alignment indicates, among beta-coronaviruses, a possible structural conservation for the region homologous to the MERS-CoV RBD core, but a high variation in the external receptor binding motif region for virus-specific pathogenesis such as receptor recognition. |
| WOS标题词 | Science & Technology |
| 类目[WOS] | Multidisciplinary Sciences |
| 研究领域[WOS] | Science & Technology - Other Topics |
| 关键词[WOS] | RESPIRATORY-SYNDROME CORONAVIRUS ; CRYSTAL-STRUCTURE ; SPIKE PROTEIN ; FUNCTIONAL RECEPTOR ; SARS CORONAVIRUS ; AMINOPEPTIDASE-N ; MIDDLE-EAST ; REVEALS ; MEMBRANE ; COMPLEX |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000322825500039 |
| 源URL | [http://124.16.173.210/handle/834782/1294]  |
| 专题 | 天津工业生物技术研究所_蛋白质工程与疫苗实验室 高福_期刊论文 |
| 作者单位 | 1.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China 2.Anhui Univ, Sch Life Sci, Hefei 230039, Peoples R China 3.Chinese Acad Sci, Inst Biophys, Lab Noncoding RNA, Beijing 100101, Peoples R China 4.Sichuan Univ, Sch Life Sci, Chengdu 610064, Sichuan, Peoples R China 5.Tianjin Inst Ind Biotechnol, Lab Prot Engn & Vaccines, Tianjin 300308, Peoples R China 6.Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Peoples R China 7.Chinese Acad Sci, Beijing Inst Life Sci, RNIH, Beijing 100101, Peoples R China 8.Chinese Ctr Dis Control & Prevent China CDC, Beijing 102206, Peoples R China |
| 推荐引用方式 GB/T 7714 | Lu, Guangwen,Hu, Yawei,Wang, Qihui,et al. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26[J]. NATURE,2013,500(7461):227-+. |
| APA | Lu, Guangwen.,Hu, Yawei.,Wang, Qihui.,Qi, Jianxun.,Gao, Feng.,...&Gao, George F..(2013).Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26.NATURE,500(7461),227-+. |
| MLA | Lu, Guangwen,et al."Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26".NATURE 500.7461(2013):227-+. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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