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Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2
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 SAR...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Published by Elsevier B.V.
2008
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114441/ https://www.ncbi.nlm.nih.gov/pubmed/18554741 http://dx.doi.org/10.1016/j.virusres.2008.03.004 |
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author | Wang, Shunxin Guo, Feng Liu, Kangtai Wang, Hongliang Rao, Shuan Yang, Peng Jiang, Chengyu |
author_facet | Wang, Shunxin Guo, Feng Liu, Kangtai Wang, Hongliang Rao, Shuan Yang, Peng Jiang, Chengyu |
author_sort | Wang, Shunxin |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-7114441 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2008 |
publisher | Published by Elsevier B.V. |
record_format | MEDLINE/PubMed |
spelling | pubmed-71144412020-04-02 Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 Wang, Shunxin Guo, Feng Liu, Kangtai Wang, Hongliang Rao, Shuan Yang, Peng Jiang, Chengyu Virus Res Article 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. Published by Elsevier B.V. 2008-09 2008-06-10 /pmc/articles/PMC7114441/ /pubmed/18554741 http://dx.doi.org/10.1016/j.virusres.2008.03.004 Text en Copyright © 2008 Published by Elsevier B.V. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Wang, Shunxin Guo, Feng Liu, Kangtai Wang, Hongliang Rao, Shuan Yang, Peng Jiang, Chengyu Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
title | Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
title_full | Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
title_fullStr | Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
title_full_unstemmed | Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
title_short | Endocytosis of the receptor-binding domain of SARS-CoV spike protein together with virus receptor ACE2 |
title_sort | endocytosis of the receptor-binding domain of sars-cov spike protein together with virus receptor ace2 |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7114441/ https://www.ncbi.nlm.nih.gov/pubmed/18554741 http://dx.doi.org/10.1016/j.virusres.2008.03.004 |
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