Proteomics

Dataset Information

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Spike Glycoprotein S1 Site-specific O-glycosylation: Systematic and Comparative Analysis from Eleven Variants of SARS CoV-2


ABSTRACT: In this study, we provide a comprehensive characterization of O-glycosylation in eleven variants of SARS-CoV-2 S1 subunit recombinantly expressed in HEK293 cells.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Homo Sapiens (human)

SUBMITTER: SHERIFDEEN ONIGBINDE  

LAB HEAD: Yehia Mechref

PROVIDER: PXD041282 | Pride | 2024-01-26

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
Alpha_1.mzXML Mzxml
Alpha_2.mzXML Mzxml
Alpha_3.mzXML Mzxml
Beta_2.mzXML Mzxml
Beta_3.mzXML Mzxml
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Publications

Variations in <i>O</i>-Glycosylation Patterns Influence Viral Pathogenicity, Infectivity, and Transmissibility in SARS-CoV-2 Variants.

Onigbinde Sherifdeen S   Reyes Cristian D Gutierrez CDG   Fowowe Mojibola M   Daramola Oluwatosin O   Atashi Mojgan M   Bennett Andrew I AI   Mechref Yehia Y  

Biomolecules 20230929 10


The highly glycosylated S protein plays a vital role in host cell invasion, making it the principal target for vaccine development. Differences in mutations observed on the spike (S) protein of SARS-CoV-2 variants may result in distinct glycosylation patterns, thus influencing immunological evasion, infectivity, and transmissibility. The glycans can mask key epitopes on the S1 protein and alter its structural conformation, allowing the virus to escape the immune system. Therefore, we comprehensi  ...[more]

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