ArticleThe Journal of biological chemistry2016
Global Mapping of O-Glycosylation of Varicella Zoster Virus, Human Cytomegalovirus, and Epstein-Barr Virus.
Article in The Journal of biological chemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed, 71 citations in OpenAlex.
- Site-specific and global glycan analysis of the human cytomegalovirus pentameric glycoprotein by high resolution mass spectrometry.Glycobiology · 2026Article
- Omics-Level Approaches to Studying Gammaherpesvirus Infection.Pathogens (Basel, Switzerland) · 2026Review
- Distinct O-Linked Glycosylation Systems in Signaling and Immune Regulation.International journal of molecular sciences · 2026Review
- Structure and immunogenicity of an engineered soluble prefusion-stabilized EBV gB antigen.Nature communications · 2026Article
- Design, Structure, and Immunogenicity of a Soluble Prefusion-stabilized EBV gB Antigen.bioRxiv : the preprint server for biology · 2025Article
- Glycoproteins gM and gN are indispensable factors for rhesus macaque rhadinovirus replication and spread but can be reconstituted by KSHV chimeras.Journal of virology · 2025Article
- Structure of the Kaposi's sarcoma-associated herpesvirus gB in post-fusion conformation.Journal of virology · 2025Article
- Human cytomegalovirus: pathogenesis, prevention, and treatment.Molecular biomedicine · 2024Review
- O-glycosylation of IgA1 and the pathogenesis of an autoimmune disease IgA nephropathy.Glycobiology · 2024Review
- Structure-based design of a soluble human cytomegalovirus glycoprotein B antigen stabilized in a prefusion-like conformation.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Sequential glycosylations at the multibasic cleavage site of SARS-CoV-2 spike protein regulate viral activity.Nature communications · 2024Article
- O-glycosylation in viruses: A sweet tango.mLife · 2024Review
- Considerations for Glycoprotein Production.Methods in molecular biology (Clifton, N.J.) · 2024Article
- Glycoengineered keratinocyte library reveals essential functions of specific glycans for all stages of HSV-1 infection.Nature communications · 2023Article
- Raman Multi-Omic Snapshot and Statistical Validation of Structural Differences between Herpes Simplex Type I and Epstein-Barr Viruses.International journal of molecular sciences · 2023Article
- O-Linked Sialoglycans Modulate the Proteolysis of SARS-CoV-2 Spike and Likely Contribute to the Mutational Trajectory in Variants of Concern.ACS central science · 2023Article
- "Glyco-sulfo barcodes" regulate chemokine receptor function.Cellular and molecular life sciences : CMLS · 2023Article
- Human cytomegalovirus induces neuronal enolase to support virally mediated metabolic remodeling.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Functional diversity: update of the posttranslational modification of Epstein-Barr virus coding proteins.Cellular and molecular life sciences : CMLS · 2022Review
- Glycan shield of the ebolavirus envelope glycoprotein GP.Communications biology · 2022Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Herpesviruses are among the most complex and widespread viruses, infection and propagation of which depend on envelope proteins. These proteins serve as mediators of cell entry as well as modulators of the immune response and are attractive vaccine targets. Although envelope proteins are known to carry glycans, little is known about the distribution, nature, and functions of these modifications. This is particularly true for O-glycans; thus we have recently developed a "bottom up" mass spectrometry-based technique for mapping O-glycosylation sites on herpes simplex virus type 1. We found wide distribution of O-glycans on herpes simplex virus type 1 glycoproteins and demonstrated that elongated O-glycans were essential for the propagation of the virus. Here, we applied our proteome-wide discovery platform for mapping O-glycosites on representative and clinically significant members of the herpesvirus family: varicella zoster virus, human cytomegalovirus, and Epstein-Barr virus. We identified a large number of O-glycosites distributed on most envelope proteins in all viruses and further demonstrated conserved patterns of O-glycans on distinct homologous proteins. Because glycosylation is highly dependent on the host cell, we tested varicella zoster virus-infected cell lysates and clinically isolated virus and found evidence of consistent O-glycosites. These results present a comprehensive view of herpesvirus O-glycosylation and point to the widespread occurrence of O-glycans in regions of envelope proteins important for virus entry, formation, and recognition by the host immune system. This knowledge enables dissection of specific functional roles of individual glycosites and, moreover, provides a framework for design of glycoprotein vaccines with representative glycosylation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.