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Viral glycoproteomes: technologies for characterization and outlook for vaccine design
- Source :
- FEBS Letters. 592:3898-3920
- Publication Year :
- 2018
- Publisher :
- Wiley, 2018.
-
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.
- Subjects :
- Proteomics
0301 basic medicine
Glycan
Glycosylation
Proteome
viruses
Biophysics
Computational biology
Biology
Biochemistry
Mass Spectrometry
Viral Proteins
03 medical and health sciences
chemistry.chemical_compound
Viral envelope
Structural Biology
Genetics
Humans
Molecular Biology
Glycoproteins
chemistry.chemical_classification
Virulence
Rational design
Viral Vaccines
Cell Biology
Glycoproteomics
carbohydrates (lipids)
030104 developmental biology
chemistry
Virus Diseases
Viruses
biology.protein
lipids (amino acids, peptides, and proteins)
Glycoprotein
Subjects
Details
- ISSN :
- 18733468 and 00145793
- Volume :
- 592
- Database :
- OpenAIRE
- Journal :
- FEBS Letters
- Accession number :
- edsair.doi.dedup.....c4afeace71574a5dadbf331936145553
- Full Text :
- https://doi.org/10.1002/1873-3468.13177