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Article

Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells

1
Copenhagen Center for Glycomics, Department of Cellular and Molecular Medicine, University of Copenhagen, 2200 Copenhagen, Denmark
2
Department of Molecular Medicine, The Scripps Research Institute, La Jolla, CA 92037, USA
3
ExpreS2ion Biotechnologies, SCION-DTU Science Park, 2970 Hørsholm, Denmark
4
Centre for Medical Parasitology at Department of Immunology and Microbiology, University of Copenhagen and Department of Infectious Diseases, Copenhagen University Hospital, 2200 Copenhagen, Denmark
5
AdaptVac Aps, 2970 Hørsholm, Denmark
6
Biognos AB, 417 05 Gothenburg, Sweden
*
Authors to whom correspondence should be addressed.
Academic Editors: Jacques Le Pendu and Göran Larson
Viruses 2021, 13(4), 551; https://doi.org/10.3390/v13040551
Received: 3 February 2021 / Revised: 16 March 2021 / Accepted: 22 March 2021 / Published: 25 March 2021
(This article belongs to the Special Issue Glycans in Viral Infection and Immunity)
Enveloped viruses hijack not only the host translation processes, but also its glycosylation machinery, and to a variable extent cover viral surface proteins with tolerogenic host-like structures. SARS-CoV-2 surface protein S presents as a trimer on the viral surface and is covered by a dense shield of N-linked glycans, and a few O-glycosites have been reported. The location of O-glycans is controlled by a large family of initiating enzymes with variable expression in cells and tissues and hence is difficult to predict. Here, we used our well-established O-glycoproteomic workflows to map the precise positions of O-linked glycosylation sites on three different entities of protein S—insect cell or human cell-produced ectodomains, or insect cell derived receptor binding domain (RBD). In total 25 O-glycosites were identified, with similar patterns in the two ectodomains of different cell origin, and a distinct pattern of the monomeric RBD. Strikingly, 16 out of 25 O-glycosites were located within three amino acids from known N-glycosites. However, O-glycosylation was primarily found on peptides that were unoccupied by N-glycans, and otherwise had low overall occupancy. This suggests possible complementary functions of O-glycans in immune shielding and negligible effects of O-glycosylation on subunit vaccine design for SARS-CoV-2. View Full-Text
Keywords: SARS-CoV-2; O-glycoproteomics; site-specific glycosylation; molecular modelling; COVID-19; GalNAc; O-glycosylation SARS-CoV-2; O-glycoproteomics; site-specific glycosylation; molecular modelling; COVID-19; GalNAc; O-glycosylation
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MDPI and ACS Style

Bagdonaite, I.; Thompson, A.J.; Wang, X.; Søgaard, M.; Fougeroux, C.; Frank, M.; Diedrich, J.K.; Yates, J.R., III; Salanti, A.; Vakhrushev, S.Y.; Paulson, J.C.; Wandall, H.H. Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells. Viruses 2021, 13, 551. https://doi.org/10.3390/v13040551

AMA Style

Bagdonaite I, Thompson AJ, Wang X, Søgaard M, Fougeroux C, Frank M, Diedrich JK, Yates JR III, Salanti A, Vakhrushev SY, Paulson JC, Wandall HH. Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells. Viruses. 2021; 13(4):551. https://doi.org/10.3390/v13040551

Chicago/Turabian Style

Bagdonaite, Ieva; Thompson, Andrew J.; Wang, Xiaoning; Søgaard, Max; Fougeroux, Cyrielle; Frank, Martin; Diedrich, Jolene K.; Yates, John R., III; Salanti, Ali; Vakhrushev, Sergey Y.; Paulson, James C.; Wandall, Hans H. 2021. "Site-Specific O-Glycosylation Analysis of SARS-CoV-2 Spike Protein Produced in Insect and Human Cells" Viruses 13, no. 4: 551. https://doi.org/10.3390/v13040551

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