Putative Receptor Binding Domain of Bat-Derived Coronavirus HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding Motifs
文献类型：期刊论文
| 作者 | Huang, Canping1; Qi, Jianxun2; Lu, Guangwen3,4; Wang, Qihui5; Yuan, Yuan6; Wu, Ying2; Zhang, Yanfang2; Yan, Jinghua5; Gao, George F.1,2,6,7,8 |
| 刊名 | BIOCHEMISTRY
 |
| 出版日期 | 2016-11-01 |
| 卷号 | 55期号:43页码:5977-5988 |
| 英文摘要 | The suggested bat origin for Middle East respiratory syndrome coronavirus (MERS-CoV) has revitalized the studies of other bat-derived coronaviruses with respect to interspecies transmission potential. Bat coronavirus (BatCoV) HKU9 is an important betacoronavirus (betaCoV) that is phylogenetically affiliated with the same genus as MERS-CoV. The bat surveillance data indicated that BatCoV HKU9 has been widely spreading and circulating in bats. This highlights the necessity of characterizing the virus for its potential to cross species barriers. The receptor binding domain (RBD) of the coronavirus spike (S) protein recognizes host receptors to mediate virus entry and is therefore a key factor determining the viral tropism and transmission capacity. In this study, the putative S RBD of BatCoV HKU9 (HKU9-RBD), which is homologous to other betaCoV RBDs that have been structurally and functionally defined, was characterized via a series of biophysical and crystallographic methods. By using surface plasmon resonance, we demonstrated that HKU9-RBD binds to neither SARS-CoV receptor ACE2 nor MERS-CoV receptor CD26. We further determined the atomic structure of HKU9-RBD, which as expected is composed of a core and an external subdomain. The core subdomain fold resembles those of other betaCoV RBDs, whereas the external subdomain is structurally unique with a single helix, explaining the inability of HKU9-RBD to react with either ACE2 or CD26. Via comparison of the available RBD structures, we further proposed a homologous intersubdomain binding mode in betaCoV RBDs that anchors the external subdomain to the core subdomain. The revealed RBD features would shed light on the evolution route of betaCoV. |
| WOS标题词 | Science & Technology ; Life Sciences & Biomedicine |
| 类目[WOS] | Biochemistry & Molecular Biology |
| 研究领域[WOS] | Biochemistry & Molecular Biology |
| 关键词[WOS] | RESPIRATORY SYNDROME CORONAVIRUS ; TO-HUMAN TRANSMISSION ; MIDDLE-EAST ; MERS-COV ; CRYSTAL-STRUCTURE ; SARS-LIKE ; FUNCTIONAL RECEPTOR ; AVIAN CORONAVIRUSES ; VIRUS ; REVEALS |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000386991800002 |
| 源URL | [http://124.16.173.210/handle/834782/2298]  |
| 专题 | 天津工业生物技术研究所_酶工程实验室 马延和 _期刊论文 |
| 作者单位 | 1.Chinese Ctr Dis Control & Prevent China CDC, Natl Inst Viral Dis Control & Prevent, Beijing 102206, Peoples R China 2.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Pathogen Microbiol & Immunol, Beijing 100101, Peoples R China 3.Sichuan Univ, WCHED, State Key Lab Biotherapy, West China Hosp, Chengdu 610041, Sichuan, Peoples R China 4.Collaborat Innovat Ctr Biotherapy, Chengdu 610041, Sichuan, Peoples R China 5.Chinese Acad Sci, Inst Microbiol, CAS Key Lab Microbial Physiol & Metab Engn, Beijing 100101, Peoples R China 6.Univ Sci & Technol China, Sch Life Sci, Hefei 230026, Anhui, Peoples R China 7.Chinese Acad Sci, Tianjin Inst Ind Biotechnol, Lab Prot Engn & Vaccines, Tianjin 300308, Peoples R China 8.Chinese Acad Sci, Beijing Inst Life Sci, RNIH, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Huang, Canping,Qi, Jianxun,Lu, Guangwen,et al. Putative Receptor Binding Domain of Bat-Derived Coronavirus HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding Motifs[J]. BIOCHEMISTRY,2016,55(43):5977-5988. |
| APA | Huang, Canping.,Qi, Jianxun.,Lu, Guangwen.,Wang, Qihui.,Yuan, Yuan.,...&Gao, George F..(2016).Putative Receptor Binding Domain of Bat-Derived Coronavirus HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding Motifs.BIOCHEMISTRY,55(43),5977-5988. |
| MLA | Huang, Canping,et al."Putative Receptor Binding Domain of Bat-Derived Coronavirus HKU9 Spike Protein: Evolution of Betacoronavirus Receptor Binding Motifs".BIOCHEMISTRY 55.43(2016):5977-5988. |
入库方式： OAI收割
来源：天津工业生物技术研究所
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