O-glycosylation in viruses: A sweet tango
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Updated: Jun 24, 2025

Engineering Antiviral Agents via Surface Plasmon Resonance
Published on: June 14, 2022
Annan Ming1,2, Jianxin Zhao3, Yihan Liu1,2
1Shandong Provincial Hospital Affiliated to Shandong First Medical University Jinan China.
Abstract:
O-glycosylation is an ancient yet underappreciated protein posttranslational modification, on which many bacteria and viruses heavily rely to perform critical biological functions involved in numerous infectious diseases or even cancer. But due to the innate complexity of O-glycosylation, research techniques have been limited to study its exact role in viral attachment and entry, assembly and exit, spreading in the host cells, and the innate and adaptive immunity of the host. Recently, the advent of many newly developed methodologies (e.g., mass spectrometry, chemical biology tools, and molecular dynamics simulations) has renewed and rekindled the interest in viral-related O-glycosylation in both viral proteins and host cells, which is further fueled by the COVID-19 pandemic. In this review, we summarize recent advances in viral-related O-glycosylation, with a particular emphasis on the mucin-type O-linked α-N-acetylgalactosamine (O-GalNAc) on viral proteins and the intracellular O-linked β-N-acetylglucosamine (O-GlcNAc) modifications on host proteins. We hope to provide valuable insights into the development of antiviral reagents or vaccines for better prevention or treatment of infectious diseases.
Insights
O-glycosylation, a vital protein modification, is crucial for viruses and bacteria in infections and cancer. New methods now enable deeper study of its role in disease and host immunity, aiding antiviral development.
Area of Science:
- Biochemistry
- Virology
- Immunology
Background:
- O-glycosylation is an understudied posttranslational modification essential for microbial functions in infectious diseases and cancer.
- Its complexity has historically limited research into its precise roles in viral pathogenesis and host immune responses.
- Recent technological advancements have revitalized interest in viral O-glycosylation, particularly in light of the COVID-19 pandemic.
Purpose of the Study:
- To review recent advancements in understanding viral-related O-glycosylation.
- To highlight the significance of mucin-type O-linked α-N-acetylgalactosamine (O-GalNAc) on viral proteins.
- To emphasize intracellular O-linked β-N-acetylglucosamine (O-GlcNAc) modifications on host proteins.
Main Methods:
- Mass spectrometry
- Chemical biology tools
- Molecular dynamics simulations
Main Results:
- Recent methodologies have overcome previous limitations in studying O-glycosylation.
- O-glycosylation plays critical roles in viral attachment, entry, assembly, exit, and host immune evasion.
- Both viral O-GalNAc and host O-GlcNAc modifications are key areas of focus.
Conclusions:
- Advances in methodologies are facilitating a deeper understanding of O-glycosylation in viral infections.
- Insights into viral and host O-glycosylation can inform the development of novel antiviral strategies and vaccines.
- Further research holds promise for improved prevention and treatment of infectious diseases.
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