Glycan Recognition in Human Norovirus Infections

Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood grou...
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Autor*in:	Victoria R. Tenge [verfasserIn] Liya Hu [verfasserIn] B. V. Venkataram Prasad [verfasserIn] Göran Larson [verfasserIn] Robert L. Atmar [verfasserIn] Mary K. Estes [verfasserIn] Sasirekha Ramani [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2021

Schlagwörter:	human noroviruses histo-blood group antigens glycoconjugates human intestinal enteroids/organoids structure host–virus interactions

Übergeordnetes Werk:	In: Viruses - MDPI AG, 2009, 13(2021), 10, p 2066
Übergeordnetes Werk:	volume:13 ; year:2021 ; number:10, p 2066

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/v13102066

Katalog-ID:	DOAJ075222833

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520			\|a Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans.
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allfields	10.3390/v13102066 doi (DE-627)DOAJ075222833 (DE-599)DOAJ5d9fb0b3c61d405b8d1f53ceced271fd DE-627 ger DE-627 rakwb eng QR1-502 Victoria R. Tenge verfasserin aut Glycan Recognition in Human Norovirus Infections 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans. human noroviruses histo-blood group antigens glycoconjugates human intestinal enteroids/organoids structure host–virus interactions Microbiology Liya Hu verfasserin aut B. V. Venkataram Prasad verfasserin aut Göran Larson verfasserin aut Robert L. Atmar verfasserin aut Mary K. Estes verfasserin aut Sasirekha Ramani verfasserin aut In Viruses MDPI AG, 2009 13(2021), 10, p 2066 (DE-627)609775871 (DE-600)2516098-9 19994915 nnns volume:13 year:2021 number:10, p 2066 https://doi.org/10.3390/v13102066 kostenfrei https://doaj.org/article/5d9fb0b3c61d405b8d1f53ceced271fd kostenfrei https://www.mdpi.com/1999-4915/13/10/2066 kostenfrei https://doaj.org/toc/1999-4915 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2021 10, p 2066
spelling	10.3390/v13102066 doi (DE-627)DOAJ075222833 (DE-599)DOAJ5d9fb0b3c61d405b8d1f53ceced271fd DE-627 ger DE-627 rakwb eng QR1-502 Victoria R. Tenge verfasserin aut Glycan Recognition in Human Norovirus Infections 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans. human noroviruses histo-blood group antigens glycoconjugates human intestinal enteroids/organoids structure host–virus interactions Microbiology Liya Hu verfasserin aut B. V. Venkataram Prasad verfasserin aut Göran Larson verfasserin aut Robert L. Atmar verfasserin aut Mary K. Estes verfasserin aut Sasirekha Ramani verfasserin aut In Viruses MDPI AG, 2009 13(2021), 10, p 2066 (DE-627)609775871 (DE-600)2516098-9 19994915 nnns volume:13 year:2021 number:10, p 2066 https://doi.org/10.3390/v13102066 kostenfrei https://doaj.org/article/5d9fb0b3c61d405b8d1f53ceced271fd kostenfrei https://www.mdpi.com/1999-4915/13/10/2066 kostenfrei https://doaj.org/toc/1999-4915 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2021 10, p 2066
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allfieldsSound	10.3390/v13102066 doi (DE-627)DOAJ075222833 (DE-599)DOAJ5d9fb0b3c61d405b8d1f53ceced271fd DE-627 ger DE-627 rakwb eng QR1-502 Victoria R. Tenge verfasserin aut Glycan Recognition in Human Norovirus Infections 2021 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans. human noroviruses histo-blood group antigens glycoconjugates human intestinal enteroids/organoids structure host–virus interactions Microbiology Liya Hu verfasserin aut B. V. Venkataram Prasad verfasserin aut Göran Larson verfasserin aut Robert L. Atmar verfasserin aut Mary K. Estes verfasserin aut Sasirekha Ramani verfasserin aut In Viruses MDPI AG, 2009 13(2021), 10, p 2066 (DE-627)609775871 (DE-600)2516098-9 19994915 nnns volume:13 year:2021 number:10, p 2066 https://doi.org/10.3390/v13102066 kostenfrei https://doaj.org/article/5d9fb0b3c61d405b8d1f53ceced271fd kostenfrei https://www.mdpi.com/1999-4915/13/10/2066 kostenfrei https://doaj.org/toc/1999-4915 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_95 GBV_ILN_105 GBV_ILN_110 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_206 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_2005 GBV_ILN_2009 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2055 GBV_ILN_2111 GBV_ILN_4012 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4700 AR 13 2021 10, p 2066
language	English
source	In Viruses 13(2021), 10, p 2066 volume:13 year:2021 number:10, p 2066
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topic_facet	human noroviruses histo-blood group antigens glycoconjugates human intestinal enteroids/organoids structure host–virus interactions Microbiology
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authorswithroles_txt_mv	Victoria R. Tenge @@aut@@ Liya Hu @@aut@@ B. V. Venkataram Prasad @@aut@@ Göran Larson @@aut@@ Robert L. Atmar @@aut@@ Mary K. Estes @@aut@@ Sasirekha Ramani @@aut@@
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callnumber-first	Q - Science
author	Victoria R. Tenge
spellingShingle	Victoria R. Tenge misc QR1-502 misc human noroviruses misc histo-blood group antigens misc glycoconjugates misc human intestinal enteroids/organoids misc structure misc host–virus interactions misc Microbiology Glycan Recognition in Human Norovirus Infections
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topic_title	QR1-502 Glycan Recognition in Human Norovirus Infections human noroviruses histo-blood group antigens glycoconjugates human intestinal enteroids/organoids structure host–virus interactions
topic	misc QR1-502 misc human noroviruses misc histo-blood group antigens misc glycoconjugates misc human intestinal enteroids/organoids misc structure misc host–virus interactions misc Microbiology
topic_unstemmed	misc QR1-502 misc human noroviruses misc histo-blood group antigens misc glycoconjugates misc human intestinal enteroids/organoids misc structure misc host–virus interactions misc Microbiology
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title	Glycan Recognition in Human Norovirus Infections
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title_sort	glycan recognition in human norovirus infections
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title_auth	Glycan Recognition in Human Norovirus Infections
abstract	Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans.
abstractGer	Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans.
abstract_unstemmed	Recognition of cell-surface glycans is an important step in the attachment of several viruses to susceptible host cells. The molecular basis of glycan interactions and their functional consequences are well studied for human norovirus (HuNoV), an important gastrointestinal pathogen. Histo-blood group antigens (HBGAs), a family of fucosylated carbohydrate structures that are present on the cell surface, are utilized by HuNoVs to initially bind to cells. In this review, we describe the discovery of HBGAs as genetic susceptibility factors for HuNoV infection and review biochemical and structural studies investigating HuNoV binding to different HBGA glycans. Recently, human intestinal enteroids (HIEs) were developed as a laboratory cultivation system for HuNoV. We review how the use of this novel culture system has confirmed that fucosylated HBGAs are necessary and sufficient for infection by several HuNoV strains, describe mechanisms of antibody-mediated neutralization of infection that involve blocking of HuNoV binding to HBGAs, and discuss the potential for using the HIE model to answer unresolved questions on viral interactions with HBGAs and other glycans.
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title_short	Glycan Recognition in Human Norovirus Infections
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