The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2

Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoono...
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Autor*in:	Joel D. Allen [verfasserIn] Dylan P. Ivory [verfasserIn] Sophie Ge Song [verfasserIn] Wan-ting He [verfasserIn] Tazio Capozzola [verfasserIn] Peter Yong [verfasserIn] Dennis R. Burton [verfasserIn] Raiees Andrabi [verfasserIn] Max Crispin [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2023

Schlagwörter:	CP: Microbiology CP: Immunology

Übergeordnetes Werk:	In: Cell Reports - Elsevier, 2015, 42(2023), 4, Seite 112307-
Übergeordnetes Werk:	volume:42 ; year:2023 ; number:4 ; pages:112307-

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.1016/j.celrep.2023.112307

Katalog-ID:	DOAJ087534843

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author_variant	j d a jda d p i dpi s g s sgs w t h wth t c tc p y py d r b drb r a ra m c mc
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publishDate	2023
allfields	10.1016/j.celrep.2023.112307 doi (DE-627)DOAJ087534843 (DE-599)DOAJ405e228400594cf194fcb190e4c52c6f DE-627 ger DE-627 rakwb eng QH301-705.5 Joel D. Allen verfasserin aut The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response. CP: Microbiology CP: Immunology Biology (General) Dylan P. Ivory verfasserin aut Sophie Ge Song verfasserin aut Wan-ting He verfasserin aut Tazio Capozzola verfasserin aut Peter Yong verfasserin aut Dennis R. Burton verfasserin aut Raiees Andrabi verfasserin aut Max Crispin verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 4, Seite 112307- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:4 pages:112307- https://doi.org/10.1016/j.celrep.2023.112307 kostenfrei https://doaj.org/article/405e228400594cf194fcb190e4c52c6f kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723003182 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 4 112307-
spelling	10.1016/j.celrep.2023.112307 doi (DE-627)DOAJ087534843 (DE-599)DOAJ405e228400594cf194fcb190e4c52c6f DE-627 ger DE-627 rakwb eng QH301-705.5 Joel D. Allen verfasserin aut The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response. CP: Microbiology CP: Immunology Biology (General) Dylan P. Ivory verfasserin aut Sophie Ge Song verfasserin aut Wan-ting He verfasserin aut Tazio Capozzola verfasserin aut Peter Yong verfasserin aut Dennis R. Burton verfasserin aut Raiees Andrabi verfasserin aut Max Crispin verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 4, Seite 112307- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:4 pages:112307- https://doi.org/10.1016/j.celrep.2023.112307 kostenfrei https://doaj.org/article/405e228400594cf194fcb190e4c52c6f kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723003182 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 4 112307-
allfields_unstemmed	10.1016/j.celrep.2023.112307 doi (DE-627)DOAJ087534843 (DE-599)DOAJ405e228400594cf194fcb190e4c52c6f DE-627 ger DE-627 rakwb eng QH301-705.5 Joel D. Allen verfasserin aut The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response. CP: Microbiology CP: Immunology Biology (General) Dylan P. Ivory verfasserin aut Sophie Ge Song verfasserin aut Wan-ting He verfasserin aut Tazio Capozzola verfasserin aut Peter Yong verfasserin aut Dennis R. Burton verfasserin aut Raiees Andrabi verfasserin aut Max Crispin verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 4, Seite 112307- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:4 pages:112307- https://doi.org/10.1016/j.celrep.2023.112307 kostenfrei https://doaj.org/article/405e228400594cf194fcb190e4c52c6f kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723003182 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 4 112307-
allfieldsGer	10.1016/j.celrep.2023.112307 doi (DE-627)DOAJ087534843 (DE-599)DOAJ405e228400594cf194fcb190e4c52c6f DE-627 ger DE-627 rakwb eng QH301-705.5 Joel D. Allen verfasserin aut The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response. CP: Microbiology CP: Immunology Biology (General) Dylan P. Ivory verfasserin aut Sophie Ge Song verfasserin aut Wan-ting He verfasserin aut Tazio Capozzola verfasserin aut Peter Yong verfasserin aut Dennis R. Burton verfasserin aut Raiees Andrabi verfasserin aut Max Crispin verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 4, Seite 112307- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:4 pages:112307- https://doi.org/10.1016/j.celrep.2023.112307 kostenfrei https://doaj.org/article/405e228400594cf194fcb190e4c52c6f kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723003182 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 4 112307-
allfieldsSound	10.1016/j.celrep.2023.112307 doi (DE-627)DOAJ087534843 (DE-599)DOAJ405e228400594cf194fcb190e4c52c6f DE-627 ger DE-627 rakwb eng QH301-705.5 Joel D. Allen verfasserin aut The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 2023 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response. CP: Microbiology CP: Immunology Biology (General) Dylan P. Ivory verfasserin aut Sophie Ge Song verfasserin aut Wan-ting He verfasserin aut Tazio Capozzola verfasserin aut Peter Yong verfasserin aut Dennis R. Burton verfasserin aut Raiees Andrabi verfasserin aut Max Crispin verfasserin aut In Cell Reports Elsevier, 2015 42(2023), 4, Seite 112307- (DE-627)684964562 (DE-600)2649101-1 22111247 nnns volume:42 year:2023 number:4 pages:112307- https://doi.org/10.1016/j.celrep.2023.112307 kostenfrei https://doaj.org/article/405e228400594cf194fcb190e4c52c6f kostenfrei http://www.sciencedirect.com/science/article/pii/S2211124723003182 kostenfrei https://doaj.org/toc/2211-1247 Journal toc kostenfrei GBV_USEFLAG_A SYSFLAG_A GBV_DOAJ SSG-OLC-PHA 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_230 GBV_ILN_285 GBV_ILN_293 GBV_ILN_602 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2038 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2068 GBV_ILN_2088 GBV_ILN_2110 GBV_ILN_2112 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2153 GBV_ILN_2190 GBV_ILN_2470 GBV_ILN_2507 GBV_ILN_4012 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4126 GBV_ILN_4249 GBV_ILN_4251 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_4326 GBV_ILN_4333 GBV_ILN_4338 GBV_ILN_4367 GBV_ILN_4393 GBV_ILN_4700 AR 42 2023 4 112307-
language	English
source	In Cell Reports 42(2023), 4, Seite 112307- volume:42 year:2023 number:4 pages:112307-
sourceStr	In Cell Reports 42(2023), 4, Seite 112307- volume:42 year:2023 number:4 pages:112307-
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	CP: Microbiology CP: Immunology Biology (General)
isfreeaccess_bool	true
container_title	Cell Reports
authorswithroles_txt_mv	Joel D. Allen @@aut@@ Dylan P. Ivory @@aut@@ Sophie Ge Song @@aut@@ Wan-ting He @@aut@@ Tazio Capozzola @@aut@@ Peter Yong @@aut@@ Dennis R. Burton @@aut@@ Raiees Andrabi @@aut@@ Max Crispin @@aut@@
publishDateDaySort_date	2023-01-01T00:00:00Z
hierarchy_top_id	684964562
id	DOAJ087534843
language_de	englisch
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callnumber-first	Q - Science
author	Joel D. Allen
spellingShingle	Joel D. Allen misc QH301-705.5 misc CP: Microbiology misc CP: Immunology misc Biology (General) The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
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topic_title	QH301-705.5 The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 CP: Microbiology CP: Immunology
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title	The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
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title_full	The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
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author_browse	Joel D. Allen Dylan P. Ivory Sophie Ge Song Wan-ting He Tazio Capozzola Peter Yong Dennis R. Burton Raiees Andrabi Max Crispin
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title_sort	diversity of the glycan shield of sarbecoviruses related to sars-cov-2
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title_auth	The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
abstract	Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response.
abstractGer	Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response.
abstract_unstemmed	Summary: Animal reservoirs of sarbecoviruses represent a significant risk of emergent pandemics, as evidenced by the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) pandemic. Vaccines remain successful at limiting severe disease and death, but the potential for further coronavirus zoonosis motivates the search for pan-coronavirus vaccines. This necessitates a better understanding of the glycan shields of coronaviruses, which can occlude potential antibody epitopes on spike glycoproteins. Here, we compare the structure of 12 sarbecovirus glycan shields. Of the 22 N-linked glycan attachment sites present on SARS-CoV-2, 15 are shared by all 12 sarbecoviruses. However, there are significant differences in the processing state at glycan sites in the N-terminal domain, such as N165. Conversely, glycosylation sites in the S2 domain are highly conserved and contain a low abundance of oligomannose-type glycans, suggesting a low glycan shield density. The S2 domain may therefore provide a more attractive target for immunogen design efforts aiming to generate a pan-coronavirus antibody response.
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title_short	The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2
url	https://doi.org/10.1016/j.celrep.2023.112307 https://doaj.org/article/405e228400594cf194fcb190e4c52c6f http://www.sciencedirect.com/science/article/pii/S2211124723003182 https://doaj.org/toc/2211-1247
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The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2

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