ArticleBiochemical and biophysical research communications2021
SARS-CoV-2 spike protein receptor-binding domain N-glycans facilitate viral internalization in respiratory epithelial cells.
Article in Biochemical and biophysical research communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 22 citations in OpenAlex.
- Investigating the effects and underlying mechanisms of glycosylation sites on the immunogenicity of COVID-19 vaccines.Signal transduction and targeted therapy · 2026Article
- Development of a self-assembling multimeric Bann-RBD fusion protein in Pichia pastoris as a potential COVID-19 vaccine candidate.Scientific reports · 2025Article
- Allosteric Control and Glycan Shielding Adaptations in the SARS-CoV-2 Spike from Early to Peak Virulence.bioRxiv : the preprint server for biology · 2025Article
- Characterization of Site-Specific N- and O-Glycopeptides from Recombinant Spike and ACE2 Glycoproteins Using LC-MS/MS Analysis.International journal of molecular sciences · 2024Article
- The accomplices: Heparan sulfates and N-glycans foster SARS-CoV-2 spike:ACE2 receptor binding and virus priming.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Variations inBiomolecules · 2023Article
- 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
- Identification of broad, potent antibodies to functionally constrained regions of SARS-CoV-2 spike following a breakthrough infection.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Development of an instrument-free and low-cost ELISA dot-blot test to detect antibodies against SARS-CoV-2.Open life sciences · 2023Article
- Synthesis, Processing, and Function of N-Glycans in N-Glycoproteins.Advances in neurobiology · 2023Review
- Functional Expression of the Recombinant Spike Receptor Binding Domain of SARS-CoV-2 Omicron in the Periplasm ofBioengineering (Basel, Switzerland) · 2022Article
- Role forScience advances · 2022Article
- Screening and Characterization of Shark-Derived VNARs against SARS-CoV-2 Spike RBD Protein.International journal of molecular sciences · 2022Article
- Intranasal delivery of SARS-CoV-2 spike protein is sufficient to cause olfactory damage, inflammation and olfactory dysfunction in zebrafish.Brain, behavior, and immunity · 2022Article
- Implications of the Immune Polymorphisms of the Host and the Genetic Variability of SARS-CoV-2 in the Development of COVID-19.Viruses · 2022Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
N-glycosylation plays an important role in the pathogenesis of viral infections. However, the role of SARS-CoV-2 RBD N-glycosylation in viral entry remains elusive. In this study, we expressed and purified N331 and N343 N-glycosite mutants of SARS-CoV-2 RBD. We found that de-glycosylation at N331 and N343 drastically reduces the RBD binding to ACE2. More importantly, based on qualitative and quantitative virology research methods, we show that the mutation of RBD N-glycosites interfered with SARS-CoV-2 internalization rather than attachment potentially by decreasing RBD binding to the receptors. Also, the double N-glycosites mutant (N331 + N343) showed significantly increased sensitivity against the designated RBD neutralizing antibodies. Taken together, these results suggest that N-glycosylation of SARS-CoV-2 RBD is not only critical for viral internalization into respiratory epithelial cells but also shields the virus from neutralization. It may provide new insights into the biological process of early-stage SARS-CoV-2 infection with potential therapeutic implications.
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