Ion channel structure and function of the MERS coronavirus E protein
文献类型：期刊论文
| 作者 | Sucec, Iva1; Xia, Bingqing2; Somberg, Noah H.1; Wang, Yi2; Jo, Hyunil3; Li, Shuangqu2; Perrone, Barbara4; Gao, Zhaobing2; Hong, Mei1 |
| 刊名 | SCIENCE ADVANCES
 |
| 出版日期 | 2025-07-09 |
| 卷号 | 11期号:28页码:14 |
| DOI | 10.1126/sciadv.adx1788 |
| 英文摘要 | Coronavirus envelope (E) proteins form drug-targeted ion channels that cause virulence to infected cells. The Middle East respiratory syndrome (MERS) virus has high mortality rates, but its E structure and function are unknown. We report the single-channel conductance and structure of membrane-bound MERS E protein. MERS E conducts K+ ions with a unitary conductance of 113 picosiemens, fivefold larger than the conductance of severe acute respiratory syndrome coronavirus 2 E. Solid-state nuclear magnetic resonance data indicate that the MERS E transmembrane domain forms a five-helix bundle that spans the lipid bilayer. The amino-terminal helical interface features multiple interacting phenylalanine (Phe) residues and an asparagine (Asn), whereas the carboxyl-terminal channel pore contains Phe33. Mutation of Phe17 abolished K+ conductance, whereas mutations of Phe33 and Asn15 suppressed most channel activity. These results indicate that MERS E contains two Phe-centered ion-conduction apparatuses, which likely permeate ions through cation-pi interactions, providing the structural basis for developing antiviral drugs to inhibit this pathogenic viroporin. |
| WOS关键词 | SOLID-STATE NMR ; TRANSMEMBRANE PROTON CHANNEL ; CENTERBAND-ONLY DETECTION ; CATION-PI INTERACTIONS ; SPIN-DIFFUSION ; POTASSIUM CHANNEL ; CONDUCTION ; DYNAMICS ; EXCHANGE ; ORIENTATION |
| 资助项目 | National Institutes of Health grant[U19AI171110] ; National Natural Science Foundation of China[82341058] ; NSF[1745302] |
| WOS研究方向 | Science & Technology - Other Topics |
| 语种 | 英语 |
| WOS记录号 | WOS:001525278400005 |
| 出版者 | AMER ASSOC ADVANCEMENT SCIENCE |
| 源URL | [http://119.78.100.183/handle/2S10ELR8/321072]  |
| 专题 | 国家级研究中心_原创新药研究全国重点实验室 |
| 通讯作者 | Gao, Zhaobing; Hong, Mei |
| 作者单位 | 1.MIT, Dept Chem, 170 Albany St, Cambridge, MA 02139 USA 2.Chinese Acad Sci, Shanghai Inst Mat Med, CAS Key Lab Receptor Res, State Key Lab Drug Res, Shanghai 201203, Peoples R China 3.Univ Calif San Francisco, Dept Pharmaceut Chem, 555 Mission Bay Blvd South, San Francisco, CA 94158 USA 4.Bruker Switzerland AG, Fallanden, Switzerland |
| 推荐引用方式 GB/T 7714 | Sucec, Iva,Xia, Bingqing,Somberg, Noah H.,et al. Ion channel structure and function of the MERS coronavirus E protein[J]. SCIENCE ADVANCES,2025,11(28):14. |
| APA | Sucec, Iva.,Xia, Bingqing.,Somberg, Noah H..,Wang, Yi.,Jo, Hyunil.,...&Hong, Mei.(2025).Ion channel structure and function of the MERS coronavirus E protein.SCIENCE ADVANCES,11(28),14. |
| MLA | Sucec, Iva,et al."Ion channel structure and function of the MERS coronavirus E protein".SCIENCE ADVANCES 11.28(2025):14. |
入库方式： OAI收割
来源：上海药物研究所
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