The glycosylation in SARS-CoV-2 and its receptor ACE2

Abstract Coronavirus disease 2019 (COVID-19), a highly infectious disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected more than 235 million individuals and led to more than 4.8 million deaths worldwide as of October 5 2021. Cryo-electron microscopy and topolo...

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Autores principales:	Yanqiu Gong, Suideng Qin, Lunzhi Dai, Zhixin Tian
Formato:	article
Lenguaje:	EN
Publicado:	Nature Publishing Group 2021
Materias:	Medicine R Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/cf4b63c4b5634a558818b0ef1ced039b
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spelling	oai:doaj.org-article:cf4b63c4b5634a558818b0ef1ced039b2021-11-21T12:06:59ZThe glycosylation in SARS-CoV-2 and its receptor ACE210.1038/s41392-021-00809-82059-3635https://doaj.org/article/cf4b63c4b5634a558818b0ef1ced039b2021-11-01T00:00:00Zhttps://doi.org/10.1038/s41392-021-00809-8https://doaj.org/toc/2059-3635Abstract Coronavirus disease 2019 (COVID-19), a highly infectious disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected more than 235 million individuals and led to more than 4.8 million deaths worldwide as of October 5 2021. Cryo-electron microscopy and topology show that the SARS-CoV-2 genome encodes lots of highly glycosylated proteins, such as spike (S), envelope (E), membrane (M), and ORF3a proteins, which are responsible for host recognition, penetration, binding, recycling and pathogenesis. Here we reviewed the detections, substrates, biological functions of the glycosylation in SARS-CoV-2 proteins as well as the human receptor ACE2, and also summarized the approved and undergoing SARS-CoV-2 therapeutics associated with glycosylation. This review may not only broad the understanding of viral glycobiology, but also provide key clues for the development of new preventive and therapeutic methodologies against SARS-CoV-2 and its variants.Yanqiu GongSuideng QinLunzhi DaiZhixin TianNature Publishing GrouparticleMedicineRBiology (General)QH301-705.5ENSignal Transduction and Targeted Therapy, Vol 6, Iss 1, Pp 1-24 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Biology (General) QH301-705.5
spellingShingle	Medicine R Biology (General) QH301-705.5 Yanqiu Gong Suideng Qin Lunzhi Dai Zhixin Tian The glycosylation in SARS-CoV-2 and its receptor ACE2
description	Abstract Coronavirus disease 2019 (COVID-19), a highly infectious disease caused by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), has infected more than 235 million individuals and led to more than 4.8 million deaths worldwide as of October 5 2021. Cryo-electron microscopy and topology show that the SARS-CoV-2 genome encodes lots of highly glycosylated proteins, such as spike (S), envelope (E), membrane (M), and ORF3a proteins, which are responsible for host recognition, penetration, binding, recycling and pathogenesis. Here we reviewed the detections, substrates, biological functions of the glycosylation in SARS-CoV-2 proteins as well as the human receptor ACE2, and also summarized the approved and undergoing SARS-CoV-2 therapeutics associated with glycosylation. This review may not only broad the understanding of viral glycobiology, but also provide key clues for the development of new preventive and therapeutic methodologies against SARS-CoV-2 and its variants.
format	article
author	Yanqiu Gong Suideng Qin Lunzhi Dai Zhixin Tian
author_facet	Yanqiu Gong Suideng Qin Lunzhi Dai Zhixin Tian
author_sort	Yanqiu Gong
title	The glycosylation in SARS-CoV-2 and its receptor ACE2
title_short	The glycosylation in SARS-CoV-2 and its receptor ACE2
title_full	The glycosylation in SARS-CoV-2 and its receptor ACE2
title_fullStr	The glycosylation in SARS-CoV-2 and its receptor ACE2
title_full_unstemmed	The glycosylation in SARS-CoV-2 and its receptor ACE2
title_sort	glycosylation in sars-cov-2 and its receptor ace2
publisher	Nature Publishing Group
publishDate	2021
url	https://doaj.org/article/cf4b63c4b5634a558818b0ef1ced039b
work_keys_str_mv	AT yanqiugong theglycosylationinsarscov2anditsreceptorace2 AT suidengqin theglycosylationinsarscov2anditsreceptorace2 AT lunzhidai theglycosylationinsarscov2anditsreceptorace2 AT zhixintian theglycosylationinsarscov2anditsreceptorace2 AT yanqiugong glycosylationinsarscov2anditsreceptorace2 AT suidengqin glycosylationinsarscov2anditsreceptorace2 AT lunzhidai glycosylationinsarscov2anditsreceptorace2 AT zhixintian glycosylationinsarscov2anditsreceptorace2
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The glycosylation in SARS-CoV-2 and its receptor ACE2

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