Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
| |
Authors: | Wang Shunxin Guo Feng Liu Kangtai Wang Hongliang Rao Shuan Yang Peng Jiang Chengyu |
| |
Affiliation: | National Key Laboratory of Medical Molecular Biology, School of Basic Medicine, Peking Union Medical College, Tsinghua University and Institute of Basic Medical Sciences Chinese Academy of Medical Sciences, Beijing 100005, China. |
| |
Abstract: | Cell entry of severe acute respiratory syndrome coronavirus (SARS-CoV) is mediated by the viral spike (S) protein. Amino acids 319-510 on the S protein have been mapped as the receptor-binding domain (RBD), which mediates binding to the SARS-CoV receptor angiotensin converting enzyme 2 (ACE2) on SARS-CoV susceptible cells. In this study, we expressed a fusion protein containing the human codon-optimized RBD of the SARS-CoV spike protein linked to the Fc portion of human IgG1 (named RBD-Fc) in HEK293 cells. The RBD-Fc protein was purified by affinity chromatography. The flow cytometry assay showed that the purified RBD-Fc protein could bind to ACE2. We demonstrated that the RBD spike protein alone could be internalized into SARS-CoV susceptible cells together with ACE2. We also showed that the removal of N-glycans from the RBD spike protein did not abolish this phenomenon. Our discoveries may have some implications for the development of the SARS vaccine. |
| |
Keywords: | Severe acute respiratory syndrome coronavirus (SARS-CoV) Receptor-binding domain (RBD) Endocytosis N-Linked glycosylation Angiotensin converting enzyme 2 (ACE2) |
本文献已被 ScienceDirect PubMed 等数据库收录! |