Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli
文献类型：期刊论文
| 作者 | He, Yunxia1,2; Qi, Jinming1,2; Xiao, Lucheng1,2; Shen, Lijuan2; Yu, Weili2; Hu, Tao2 |
| 刊名 | ENGINEERING IN LIFE SCIENCES
 |
| 出版日期 | 2021-05-07 |
| 页码 | 8 |
| 关键词 | COVID‐ 19 purification RBD SARS‐ CoV‐ 2 spike protein |
| ISSN号 | 1618-0240 |
| DOI | 10.1002/elsc.202000106 |
| 英文摘要 | SARS-CoV-2 is responsible for a disruptive worldwide viral pandemic, and renders a severe respiratory disease known as COVID-19. Spike protein of SARS-CoV-2 mediates viral entry into host cells by binding ACE2 through the receptor-binding domain (RBD). RBD is an important target for development of virus inhibitors, neutralizing antibodies, and vaccines. RBD expressed in mammalian cells suffers from low expression yield and high cost. E. coli is a popular host for protein expression, which has the advantage of easy scalability with low cost. However, RBD expressed by E. coli (RBD-1) lacks the glycosylation, and its antigenic epitopes may not be sufficiently exposed. In the present study, RBD-1 was expressed by E. coli and purified by a Ni Sepharose Fast Flow column. RBD-1 was structurally characterized and compared with RBD expressed by the HEK293 cells (RBD-2). The secondary structure and tertiary structure of RBD-1 were largely maintained without glycosylation. In particular, the major beta-sheet content of RBD-1 was almost unaltered. RBD-1 could strongly bind ACE2 with a dissociation constant (K-D) of 2.98 x 10(-8) M. Thus, RBD-1 was expected to apply in the vaccine development, screening drugs and virus test kit. |
| WOS关键词 | EXPRESSION |
| 资助项目 | National Key Research and Development Project ofChina ; NationalNatural Science Foundation of China[31970875] ; BeijingNatural Science Foundation |
| WOS研究方向 | Biotechnology & Applied Microbiology |
| 语种 | 英语 |
| WOS记录号 | WOS:000648189700001 |
| 出版者 | WILEY |
| 资助机构 | National Key Research and Development Project ofChina ; NationalNatural Science Foundation of China ; BeijingNatural Science Foundation |
| 源URL | [http://ir.ipe.ac.cn/handle/122111/48637]  |
| 专题 | 中国科学院过程工程研究所 |
| 通讯作者 | Yu, Weili; Hu, Tao |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing, Peoples R China 2.Chinese Acad Sci, Inst Proc Engn, State Key Lab Biochem Engn, Beijing 100190, Peoples R China |
| 推荐引用方式 GB/T 7714 | He, Yunxia,Qi, Jinming,Xiao, Lucheng,et al. Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli[J]. ENGINEERING IN LIFE SCIENCES,2021:8. |
| APA | He, Yunxia,Qi, Jinming,Xiao, Lucheng,Shen, Lijuan,Yu, Weili,&Hu, Tao.(2021).Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli.ENGINEERING IN LIFE SCIENCES,8. |
| MLA | He, Yunxia,et al."Purification and characterization of the receptor-binding domain of SARS-CoV-2 spike protein from Escherichia coli".ENGINEERING IN LIFE SCIENCES (2021):8. |
入库方式： OAI收割
来源：过程工程研究所
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