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Related Concept Videos

Protein Glycosylation01:25

Protein Glycosylation

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Glycosylation, the most common post-translational modification for proteins, serves diverse functions. Adding sugars to proteins makes the proteins more resistant to proteolytic digestion. Glycosylated proteins can act as markers and receptors to promote cell-cell adhesion. Additionally, they have many essential quality control functions in the cell, such as correct protein folding and facilitating transport of misfolded proteins to the cytosol, which can be degraded.
Glycosylation occurs in...
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Conjugated Proteins02:50

Conjugated Proteins

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Simple proteins and protein complexes contain only amino acids. In contrast, many other proteins, called conjugated proteins, covalently bond with non-protein moieties.
Nucleoproteins are protein complexes that contain nucleic acids, categorized as deoxyribonucleoproteins (DNPs) or ribonucleoproteins (RNPs) respectively. The nucleosome is a typical example of a DNP where nuclear DNA is associated with histone proteins. The major antigen for the Covid-19 virus SARS-CoV is an RNP that is critical...
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Glycocalyx and its Functions01:14

Glycocalyx and its Functions

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The glycocalyx is a carbohydrate-rich, fuzzy-appearing layer on the outer surface of the cell membrane. It is highly hydrophilic, because of this it attracts large amounts of water to the cell's surface. This aids the cell's interaction with the watery environment and also helps it to obtain substances dissolved in the water. It is also important for cell identification, self/non-self determination, and embryonic development and is used in cell-to-cell attachments to form tissues.
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Updated: Jul 24, 2025

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SARS-CoV-2 spike glycosylation affects function and neutralization sensitivity.

Fengwen Zhang1, Fabian Schmidt1,2, Frauke Muecksch1

  • 1Laboratory of Retrovirology, The Rockefeller University, New York, NY 10065, USA.

Biorxiv : the Preprint Server for Biology
|July 10, 2023
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Summary

Glycosylation of SARS-CoV-2 spike proteins impacts virus infectivity and immune evasion. While N343 glycan hinders neutralization, COVID-19 vaccination elicits resilient antibodies.

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Area of Science:

  • Virology
  • Immunology
  • Structural Biology

Background:

  • Viral envelope protein glycosylation is crucial for virus biology and immune evasion.
  • The SARS-CoV-2 spike (S) glycoprotein possesses numerous N-linked and O-linked glycosylation sites.
  • Understanding glycosylation's role is key to developing effective therapeutics and vaccines.

Approach:

  • Investigated the impact of individual glycosylation site removal on SARS-CoV-2 S glycoprotein function.
  • Utilized pseudotyped virus infection assays to measure infectivity.
  • Assessed sensitivity to monoclonal and polyclonal neutralizing antibodies from convalescent individuals and vaccinees.

Key Points:

  • Removal of most individual glycosylation sites reduced pseudotyped virus infectivity.
  • Reduced infectivity correlated with lower levels of incorporated spike protein for N-terminal domain (NTD) and receptor binding domain (RBD) mutants.
  • The N343 glycan in the RBD modulated neutralization by specific monoclonal antibodies and reduced sensitivity to polyclonal antibodies.

Conclusions:

  • SARS-CoV-2 spike glycosylation plays a significant role in immune evasion by reducing susceptibility to neutralizing antibodies.
  • While N343 glycan can be a target for neutralization, vaccination in convalescent individuals generates antibodies resistant to this glycan's inhibitory effects.
  • Glycosylation patterns are critical determinants of SARS-CoV-2 pathogenesis and host immune responses.