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...
| Main Authors: | , , , , , , , , |
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| Format: | Article |
| Language: | English |
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Elsevier
2023-04-01
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| Series: | Cell Reports |
| Subjects: | |
| Online Access: | http://www.sciencedirect.com/science/article/pii/S2211124723003182 |
| _version_ | 1797859748927766528 |
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| author | Joel D. Allen Dylan P. Ivory Sophie Ge Song Wan-ting He Tazio Capozzola Peter Yong Dennis R. Burton Raiees Andrabi Max Crispin |
| author_facet | Joel D. Allen Dylan P. Ivory Sophie Ge Song Wan-ting He Tazio Capozzola Peter Yong Dennis R. Burton Raiees Andrabi Max Crispin |
| author_sort | Joel D. Allen |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-04-09T21:34:36Z |
| format | Article |
| id | doaj.art-405e228400594cf194fcb190e4c52c6f |
| institution | Directory Open Access Journal |
| issn | 2211-1247 |
| language | English |
| last_indexed | 2024-04-09T21:34:36Z |
| publishDate | 2023-04-01 |
| publisher | Elsevier |
| record_format | Article |
| series | Cell Reports |
| spelling | doaj.art-405e228400594cf194fcb190e4c52c6f2023-03-27T04:02:54ZengElsevierCell Reports2211-12472023-04-01424112307The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2Joel D. Allen0Dylan P. Ivory1Sophie Ge Song2Wan-ting He3Tazio Capozzola4Peter Yong5Dennis R. Burton6Raiees Andrabi7Max Crispin8School of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK; Corresponding authorSchool of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UKDepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 13 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USADepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 13 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USADepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 13 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USADepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 13 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USADepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 13 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USA; Ragon Institute of Massachusetts General Hospital, Massachusetts Institute of Technology, and Harvard University, Cambridge, MA 02139, USADepartment of Immunology and Microbiology, The Scripps Research Institute, La Jolla, CA 13 92037, USA; IAVI Neutralizing Antibody Center, The Scripps Research Institute, La Jolla, CA 92037, USA; Consortium for HIV/AIDS Vaccine Development (CHAVD), The Scripps Research Institute, La Jolla, CA 92037, USASchool of Biological Sciences, University of Southampton, Southampton SO17 1BJ, UK; Corresponding authorSummary: 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.http://www.sciencedirect.com/science/article/pii/S2211124723003182CP: MicrobiologyCP: Immunology |
| spellingShingle | Joel D. Allen Dylan P. Ivory Sophie Ge Song Wan-ting He Tazio Capozzola Peter Yong Dennis R. Burton Raiees Andrabi Max Crispin The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 Cell Reports CP: Microbiology CP: Immunology |
| title | The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 |
| title_full | The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 |
| title_fullStr | The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 |
| title_full_unstemmed | The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 |
| title_short | The diversity of the glycan shield of sarbecoviruses related to SARS-CoV-2 |
| title_sort | diversity of the glycan shield of sarbecoviruses related to sars cov 2 |
| topic | CP: Microbiology CP: Immunology |
| url | http://www.sciencedirect.com/science/article/pii/S2211124723003182 |
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