ArticleScientific reports2021
N-glycosylation profiles of the SARS-CoV-2 spike D614G mutant and its ancestral protein characterized by advanced mass spectrometry.
Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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16 citing papers in PubMed, 24 citations in OpenAlex.
- Protein Complex Heterogeneity and Topology Revealed by Electron Capture Charge Reduction and Surface Induced Dissociation.ACS central science · 2024Article
- Protein complex heterogeneity and topology revealed by electron capture charge reduction and surface induced dissociation.bioRxiv : the preprint server for biology · 2024Article
- The Malaria Box molecules: a source for targeting the RBD and NTD cryptic pocket of the spike glycoprotein in SARS-CoV-2.Journal of molecular modeling · 2024Article
- Enhanced Surface Accessibility of SARS-CoV-2 Omicron Spike Protein Due to an Altered Glycosylation Profile.ACS infectious diseases · 2024Article
- The IRE1α-XBP1 arm of the unfolded protein response is a host factor activated in SARS-CoV-2 infection.Biochimica et biophysica acta. Molecular basis of disease · 2024Article
- The role of N-glycosylation in spike antigenicity for the SARS-CoV-2 gamma variant.Glycobiology · 2024Article
- Inclusion of deuterated glycopeptides provides increased sequence coverage in hydrogen/deuterium exchange mass spectrometry analysis of SARS-CoV-2 spike glycoprotein.Rapid communications in mass spectrometry : RCM · 2024Article
- Analysis of the N-glycosylation profiles of the spike proteins from the Alpha, Beta, Gamma, and Delta variants of SARS-CoV-2.Analytical and bioanalytical chemistry · 2023Article
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- Glycosylation in SARS-CoV-2 variants: A path to infection and recovery.Biochemical pharmacology · 2022Review
- Systematic analysis and comparison of O-glycosylation of five recombinant spike proteins in β-coronaviruses.Analytica chimica acta · 2022Article
- Investigation of theMolecules (Basel, Switzerland) · 2022Article
- Analysis of memory B cells identifies conserved neutralizing epitopes on the N-terminal domain of variant SARS-Cov-2 spike proteins.Immunity · 2022Article
- Conserved Neutralizing Epitopes on the N-Terminal Domain of Variant SARS-CoV-2 Spike Proteins.bioRxiv : the preprint server for biology · 2022Article
- Molecular evolution of human coronavirus-NL63, -229E, -HKU1 and -OC43 in hospitalized children in China.Frontiers in microbiology · 2022Article
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Authors and funding
15 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-glycosylation plays an important role in the structure and function of membrane and secreted proteins. The spike protein on the surface of the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2), the virus that causes COVID-19, is heavily glycosylated and the major target for developing vaccines, therapeutic drugs and diagnostic tests. The first major SARS-CoV-2 variant carries a D614G substitution in the spike (S-D614G) that has been associated with altered conformation, enhanced ACE2 binding, and increased infectivity and transmission. In this report, we used mass spectrometry techniques to characterize and compare the N-glycosylation of the wild type (S-614D) or variant (S-614G) SARS-CoV-2 spike glycoproteins prepared under identical conditions. The data showed that half of the N-glycosylation sequons changed their distribution of glycans in the S-614G variant. The S-614G variant showed a decrease in the relative abundance of complex-type glycans (up to 45%) and an increase in oligomannose glycans (up to 33%) on all altered sequons. These changes led to a reduction in the overall complexity of the total N-glycosylation profile. All the glycosylation sites with altered patterns were in the spike head while the glycosylation of three sites in the stalk remained unchanged between S-614G and S-614D proteins.
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