Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors

Summary: Glycosylation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein mediates viral entry and immune escape. While glycan site is determined by viral genetic code, glycosylation is completely dependent on host cell post-translational modification. Here, by produc...

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Autores principales:	Lei Guo, Yan Liang, Heng Li, Huiwen Zheng, Zening Yang, Yanli Chen, Xin Zhao, Jing Li, Binxiang Li, Haijing Shi, Ming Sun, Longding Liu
Formato:	article
Lenguaje:	EN
Publicado:	Elsevier 2021
Materias:	Immunity Virology Cell biology Cell Glycomics Science Q
Acceso en línea:	https://doaj.org/article/06834252cfd24c75bcb905ccb32f8147
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spelling	oai:doaj.org-article:06834252cfd24c75bcb905ccb32f81472021-11-22T04:28:52ZEpigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors2589-004210.1016/j.isci.2021.103426https://doaj.org/article/06834252cfd24c75bcb905ccb32f81472021-12-01T00:00:00Zhttp://www.sciencedirect.com/science/article/pii/S2589004221013973https://doaj.org/toc/2589-0042Summary: Glycosylation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein mediates viral entry and immune escape. While glycan site is determined by viral genetic code, glycosylation is completely dependent on host cell post-translational modification. Here, by producing SARS-CoV-2 virions from various host cell lines, viruses of different origins with diverse spike protein glycan patterns were revealed. Binding affinities to C-type lectin receptors (CLRs) DC&L-SIGN differed in the different glycan pattern virions. Although none of the CLRs supported viral productive infection, viral trans&cis-infection mediated by the CLRs were substantially changed among the different virions. Specifically, trans&cis-infection of virions with a high-mannose structure (Man5GlcNAc2) at the N1098 glycan site of the spike postfusion trimer were markedly enhanced. Considering L-SIGN co-expression with ACE2 on respiratory tract cells, our work underlines viral epigenetic glycosylation in authentic viral infection and highlights the attachment co-receptor role of DC&L-SIGN in SARS-CoV-2 infection and prevention.Lei GuoYan LiangHeng LiHuiwen ZhengZening YangYanli ChenXin ZhaoJing LiBinxiang LiHaijing ShiMing SunLongding LiuElsevierarticleImmunityVirologyCell biologyCellGlycomicsScienceQENiScience, Vol 24, Iss 12, Pp 103426- (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunity Virology Cell biology Cell Glycomics Science Q
spellingShingle	Immunity Virology Cell biology Cell Glycomics Science Q Lei Guo Yan Liang Heng Li Huiwen Zheng Zening Yang Yanli Chen Xin Zhao Jing Li Binxiang Li Haijing Shi Ming Sun Longding Liu Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
description	Summary: Glycosylation of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) spike glycoprotein mediates viral entry and immune escape. While glycan site is determined by viral genetic code, glycosylation is completely dependent on host cell post-translational modification. Here, by producing SARS-CoV-2 virions from various host cell lines, viruses of different origins with diverse spike protein glycan patterns were revealed. Binding affinities to C-type lectin receptors (CLRs) DC&L-SIGN differed in the different glycan pattern virions. Although none of the CLRs supported viral productive infection, viral trans&cis-infection mediated by the CLRs were substantially changed among the different virions. Specifically, trans&cis-infection of virions with a high-mannose structure (Man5GlcNAc2) at the N1098 glycan site of the spike postfusion trimer were markedly enhanced. Considering L-SIGN co-expression with ACE2 on respiratory tract cells, our work underlines viral epigenetic glycosylation in authentic viral infection and highlights the attachment co-receptor role of DC&L-SIGN in SARS-CoV-2 infection and prevention.
format	article
author	Lei Guo Yan Liang Heng Li Huiwen Zheng Zening Yang Yanli Chen Xin Zhao Jing Li Binxiang Li Haijing Shi Ming Sun Longding Liu
author_facet	Lei Guo Yan Liang Heng Li Huiwen Zheng Zening Yang Yanli Chen Xin Zhao Jing Li Binxiang Li Haijing Shi Ming Sun Longding Liu
author_sort	Lei Guo
title	Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
title_short	Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
title_full	Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
title_fullStr	Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
title_full_unstemmed	Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors
title_sort	epigenetic glycosylation of sars-cov-2 impact viral infection through dc&l-sign receptors
publisher	Elsevier
publishDate	2021
url	https://doaj.org/article/06834252cfd24c75bcb905ccb32f8147
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Epigenetic glycosylation of SARS-CoV-2 impact viral infection through DC&L-SIGN receptors

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