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Cell entry by SARS-CoV-2

Severe acute respiratory syndrome virus 2 (SARS-CoV-2) invades host cells by interacting with receptors/coreceptors, as well as with other cofactors, via its spike (S) protein that further mediates fusion between viral and cellular membranes. The host membrane protein, angiotensin-converting enzyme...

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Detalles Bibliográficos
Autores principales: Peng, Ruchao, Wu, Lian-Ao, Wang, Qingling, Qi, Jianxun, Gao, George Fu
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Elsevier Ltd. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8180548/
https://www.ncbi.nlm.nih.gov/pubmed/34187722
http://dx.doi.org/10.1016/j.tibs.2021.06.001
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author Peng, Ruchao
Wu, Lian-Ao
Wang, Qingling
Qi, Jianxun
Gao, George Fu
author_facet Peng, Ruchao
Wu, Lian-Ao
Wang, Qingling
Qi, Jianxun
Gao, George Fu
author_sort Peng, Ruchao
collection PubMed
description Severe acute respiratory syndrome virus 2 (SARS-CoV-2) invades host cells by interacting with receptors/coreceptors, as well as with other cofactors, via its spike (S) protein that further mediates fusion between viral and cellular membranes. The host membrane protein, angiotensin-converting enzyme 2 (ACE2), is the major receptor for SARS-CoV-2 and is a crucial determinant for cross-species transmission. In addition, some auxiliary receptors and cofactors are also involved that expand the host/tissue tropism of SARS-CoV-2. After receptor engagement, specific proteases are required that cleave the S protein and trigger its fusogenic activity. Here we discuss the recent advances in understanding the molecular events during SARS-CoV-2 entry which will contribute to developing vaccines and therapeutics.
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spelling pubmed-81805482021-06-07 Cell entry by SARS-CoV-2 Peng, Ruchao Wu, Lian-Ao Wang, Qingling Qi, Jianxun Gao, George Fu Trends Biochem Sci Review Severe acute respiratory syndrome virus 2 (SARS-CoV-2) invades host cells by interacting with receptors/coreceptors, as well as with other cofactors, via its spike (S) protein that further mediates fusion between viral and cellular membranes. The host membrane protein, angiotensin-converting enzyme 2 (ACE2), is the major receptor for SARS-CoV-2 and is a crucial determinant for cross-species transmission. In addition, some auxiliary receptors and cofactors are also involved that expand the host/tissue tropism of SARS-CoV-2. After receptor engagement, specific proteases are required that cleave the S protein and trigger its fusogenic activity. Here we discuss the recent advances in understanding the molecular events during SARS-CoV-2 entry which will contribute to developing vaccines and therapeutics. Elsevier Ltd. 2021-10 2021-06-07 /pmc/articles/PMC8180548/ /pubmed/34187722 http://dx.doi.org/10.1016/j.tibs.2021.06.001 Text en © 2021 Elsevier Ltd. All rights reserved. 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 Review
Peng, Ruchao
Wu, Lian-Ao
Wang, Qingling
Qi, Jianxun
Gao, George Fu
Cell entry by SARS-CoV-2
title Cell entry by SARS-CoV-2
title_full Cell entry by SARS-CoV-2
title_fullStr Cell entry by SARS-CoV-2
title_full_unstemmed Cell entry by SARS-CoV-2
title_short Cell entry by SARS-CoV-2
title_sort cell entry by sars-cov-2
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8180548/
https://www.ncbi.nlm.nih.gov/pubmed/34187722
http://dx.doi.org/10.1016/j.tibs.2021.06.001
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