The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans

The spike protein receptor-binding domain (RBD) of SARS-CoV-2 is required for the infection of human cells. It is the main target that elicits neutralizing antibodies and also a major component of diagnostic kits. The large demand for this protein has led to the use of plants as a production platfor...

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Autores: Sobrino-Mengual, Guillermo, Armario-Najera, Victoria, Balieu, Juliette, Walet-Balieu, Marie-Laure, Saba-Mayoral, Andrea, Pelacho Aja, Ana Mª, Capell Capell, Teresa, Christou, Paul, Bardor, Muriel, Lerouge, Patrice
Formato: artículo
Estado:Versión publicada
Fecha de publicación:2024
País:España
Recursos:Universitat de Lleida (UdL)
Repositorio:Repositori Obert UdL
OAI Identifier:oai:repositori.udl.cat:10459.1/465825
Acesso em linha:https://doi.org/10.3390/ijms25084466
https://hdl.handle.net/10459.1/465825
Access Level:acceso abierto
Palavra-chave:Plant molecular farming
Receptor-binding domain
Glycan profile
Biologics
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spelling The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycansSobrino-Mengual, GuillermoArmario-Najera, VictoriaBalieu, JulietteWalet-Balieu, Marie-LaureSaba-Mayoral, AndreaPelacho Aja, Ana MªCapell Capell, TeresaChristou, PaulBardor, MurielLerouge, PatricePlant molecular farmingReceptor-binding domainGlycan profileBiologicsThe spike protein receptor-binding domain (RBD) of SARS-CoV-2 is required for the infection of human cells. It is the main target that elicits neutralizing antibodies and also a major component of diagnostic kits. The large demand for this protein has led to the use of plants as a production platform. However, it is necessary to determine the N-glycan structures of an RBD to investigate its efficacy and functionality as a vaccine candidate or diagnostic reagent. Here, we analyzed the N-glycan profile of the RBD produced in rice callus. Of the two potential N-glycan acceptor sites, we found that one was not utilized and the other contained a mixture of complex-type N-glycans. This differs from the heterogeneous mixture of N-glycans found when an RBD is expressed in other hosts, including Nicotiana benthamiana. By comparing the glycosylation profiles of different hosts, we can select platforms that produce RBDs with the most beneficial N-glycan structures for different applications.: We acknowledge funding from the Spanish Ministry of Science and Innovation MCIN/AEI/ 10.13039/501100011033/FEDER EU to project PID2022-1414160B-I00 and by Generalitat de Catalunya Grant 2021 SGR 01501 to the Agricultural Biotechnology and Bioeconomy Unit (ABBU). This research was funded by the European Union’s Horizon 2020 Research and Innovation Program through the Pharma-Factory project under Grant No. 774078. This work was also financially supported by the French government through the ANR agency under the ANR PRCE DAGENTA project (ANR-21- CE20-0038-001) and the program «Grand défi Biomédicament: améliorer les rendements et maîtriser les coûts de production: Nouveaux Systèmes d’Expression—2020» (PHAEOMABS project—ANR-21- F2II-0005). We acknowledge the Spanish Ministry of Science, Innovation and Universities for their FPI fellowship PRE2019-088852 given to GSM.MDPI2024info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttps://doi.org/10.3390/ijms25084466https://hdl.handle.net/10459.1/465825reponame:Repositori Obert UdL instname:Universitat de Lleida (UdL)Inglésinfo:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-1414160B-I00Reproducció del document publicat a: https://doi.org/10.3390/ijms25084466International Journal of Molecular Sciences, 2024, vol.25, núm. 8, p. 1-13info:eu-repo/grantAgreement/EC/H2020/774078cc-by, (c) Sobrino-Mengual et al., 2024Attribution 4.0 Internationalinfo:eu-repo/semantics/openAccesshttp://creativecommons.org/licenses/by/4.0/oai:repositori.udl.cat:10459.1/4658252026-06-24T12:42:17Z
dc.title.none.fl_str_mv The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
title The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
spellingShingle The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
Sobrino-Mengual, Guillermo
Plant molecular farming
Receptor-binding domain
Glycan profile
Biologics
title_short The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
title_full The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
title_fullStr The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
title_full_unstemmed The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
title_sort The SARS-CoV-2 spike protein receptor-binding domain expressed in rice callus features a homogeneous mix of complex-type glycans
dc.creator.none.fl_str_mv Sobrino-Mengual, Guillermo
Armario-Najera, Victoria
Balieu, Juliette
Walet-Balieu, Marie-Laure
Saba-Mayoral, Andrea
Pelacho Aja, Ana Mª
Capell Capell, Teresa
Christou, Paul
Bardor, Muriel
Lerouge, Patrice
author Sobrino-Mengual, Guillermo
author_facet Sobrino-Mengual, Guillermo
Armario-Najera, Victoria
Balieu, Juliette
Walet-Balieu, Marie-Laure
Saba-Mayoral, Andrea
Pelacho Aja, Ana Mª
Capell Capell, Teresa
Christou, Paul
Bardor, Muriel
Lerouge, Patrice
author_role author
author2 Armario-Najera, Victoria
Balieu, Juliette
Walet-Balieu, Marie-Laure
Saba-Mayoral, Andrea
Pelacho Aja, Ana Mª
Capell Capell, Teresa
Christou, Paul
Bardor, Muriel
Lerouge, Patrice
author2_role author
author
author
author
author
author
author
author
author
dc.subject.none.fl_str_mv Plant molecular farming
Receptor-binding domain
Glycan profile
Biologics
topic Plant molecular farming
Receptor-binding domain
Glycan profile
Biologics
description The spike protein receptor-binding domain (RBD) of SARS-CoV-2 is required for the infection of human cells. It is the main target that elicits neutralizing antibodies and also a major component of diagnostic kits. The large demand for this protein has led to the use of plants as a production platform. However, it is necessary to determine the N-glycan structures of an RBD to investigate its efficacy and functionality as a vaccine candidate or diagnostic reagent. Here, we analyzed the N-glycan profile of the RBD produced in rice callus. Of the two potential N-glycan acceptor sites, we found that one was not utilized and the other contained a mixture of complex-type N-glycans. This differs from the heterogeneous mixture of N-glycans found when an RBD is expressed in other hosts, including Nicotiana benthamiana. By comparing the glycosylation profiles of different hosts, we can select platforms that produce RBDs with the most beneficial N-glycan structures for different applications.
publishDate 2024
dc.date.none.fl_str_mv 2024
dc.type.none.fl_str_mv info:eu-repo/semantics/article
info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.none.fl_str_mv https://doi.org/10.3390/ijms25084466
https://hdl.handle.net/10459.1/465825
url https://doi.org/10.3390/ijms25084466
https://hdl.handle.net/10459.1/465825
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv info:eu-repo/grantAgreement/AEI/Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023/PID2022-1414160B-I00
Reproducció del document publicat a: https://doi.org/10.3390/ijms25084466
International Journal of Molecular Sciences, 2024, vol.25, núm. 8, p. 1-13
info:eu-repo/grantAgreement/EC/H2020/774078
dc.rights.none.fl_str_mv cc-by, (c) Sobrino-Mengual et al., 2024
Attribution 4.0 International
info:eu-repo/semantics/openAccess
http://creativecommons.org/licenses/by/4.0/
rights_invalid_str_mv cc-by, (c) Sobrino-Mengual et al., 2024
Attribution 4.0 International
http://creativecommons.org/licenses/by/4.0/
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv MDPI
publisher.none.fl_str_mv MDPI
dc.source.none.fl_str_mv reponame:Repositori Obert UdL
instname:Universitat de Lleida (UdL)
instname_str Universitat de Lleida (UdL)
reponame_str Repositori Obert UdL
collection Repositori Obert UdL
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,812429

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