Viral glycoproteomes: technologies for characterization and outlook for vaccine design

FEBS Lett. 2018 Dec;592(23):3898-3920. doi: 10.1002/1873-3468.13177. Epub 2018 Jul 12.

Abstract

It has long been known that surface proteins of most enveloped viruses are covered with glycans. It has furthermore been demonstrated that glycosylation is essential for propagation and immune evasion for many viruses. The recent development of high-resolution mass spectrometry techniques has enabled identification not only of the precise structures but also the positions of such post-translational modifications on viruses, revealing substantial differences in extent of glycosylation and glycan maturation for different classes of viruses. In-depth characterization of glycosylation and other post-translational modifications of viral envelope glycoproteins is essential for rational design of vaccines and antivirals. In this Review, we provide an overview of techniques used to address viral glycosylation and summarize information on glycosylation of enveloped viruses representing ongoing public health challenges. Furthermore, we discuss how knowledge on glycosylation can be translated to means to prevent and combat viral infections.

Keywords: enveloped virus; glycoproteomics; mass spectrometry; site-specific glycosylation; virus glycosylation.

Publication types

  • Review

MeSH terms

  • Glycoproteins / metabolism*
  • Humans
  • Mass Spectrometry / methods
  • Proteome / metabolism*
  • Proteomics / methods*
  • Viral Proteins / metabolism*
  • Viral Vaccines / immunology
  • Virulence / immunology
  • Virus Diseases / immunology
  • Virus Diseases / virology
  • Viruses / immunology
  • Viruses / metabolism
  • Viruses / pathogenicity

Substances

  • Glycoproteins
  • Proteome
  • Viral Proteins
  • Viral Vaccines

Associated data

  • GENBANK/KM233105.1