Exploitation of glycosylation in enveloped virus pathobiology

Abstract

Glycosylation is a ubiquitous post-translational modification responsible for a multitude of crucial biological roles. As obligate parasites, viruses exploit host-cell machinery to glycosylate their own proteins during replication. Viral envelope proteins from a variety of human pathogens including HIV-1, influenza virus, Lassa virus, SARS, Zika virus, dengue virus, and Ebola virus have evolved to be extensively glycosylated. These host-cell derived glycans facilitate diverse structural and functional roles during the viral life-cycle, ranging from immune evasion by glycan shielding to enhancement of immune cell infection. In this review, we highlight the imperative and auxiliary roles glycans play, and how specific oligosaccharide structures facilitate these functions during viral pathogenesis. We discuss the growing efforts to exploit viral glycobiology in the development of anti-viral vaccines and therapies.

Cited by papers we hold 16

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• Biosynthesis of α-Gal Epitopes (Galα1-3Galβ1-4GlcNAc-R) and Their Unique Potential in Future α-Gal Therapies · 2021
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• Assessing Antigen Structural Integrity through Glycosylation Analysis of the SARS-CoV‑2 Viral Spike · 2021
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• The Case for S2: The Potential Benefits of the S2 Subunit of the SARS-CoV-2 Spike Protein as an Immunogen in Fighting the COVID-19 Pandemic · 2021
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• Native-like SARS-CoV-2 Spike Glycoprotein Expressed by ChAdOx1 nCoV-19/AZD1222 Vaccine · 2021
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• Computational epitope map of SARS-CoV-2 spike protein · 2021
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• The flexibility of ACE2 in the context of SARS-CoV-2 infection · 2021
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• The glycosylation in SARS-CoV-2 and its receptor ACE2 · 2021
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• Emerging COVID-19 coronavirus: glycan shield and structure prediction of spike glycoprotein and its interaction with human CD26 · 2020
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• Site-specific glycan analysis of the SARS-CoV-2 spike · 2020
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• Vulnerabilities in coronavirus glycan shields despite extensive glycosylation · 2020
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