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The N-glycosylation of Equine Tetherin Affects Antiviral Activity by Regulating Its Subcellular Localization
- Source :
- Viruses, Volume 12, Issue 2, Viruses, Vol 12, Iss 2, p 220 (2020)
- Publication Year :
- 2020
- Publisher :
- Multidisciplinary Digital Publishing Institute, 2020.
-
Abstract
- Tetherin is an interferon-inducible type II transmembrane glycoprotein which inhibits the release of viruses, including retroviruses, through a &ldquo<br />physical tethering&rdquo<br />model. However, the role that the glycosylation of tetherin plays in its antiviral activity remains controversial. In this study, we found that mutation of N-glycosylation sites resulted in an attenuation of the antiviral activity of equine tetherin (eqTHN), as well as a reduction in the expression of eqTHN at the plasma membrane (PM). In addition, eqTHN N-glycosylation mutants colocalize obviously with ER, CD63, LAMP1 and endosomes, while WT eqTHN do not. Furthermore, we also found that N-glycosylation impacts the transport of eqTHN in the cell not by affecting the endocytosis, but rather by influencing the anterograde trafficking of the protein. These results suggest that the N-glycosylation of eqTHN is important for the antiviral activity of the protein through regulating its normal subcellular localization. This finding will enhance our understanding of the function of this important restriction factor.
- Subjects :
- 0301 basic medicine
Glycosylation
Endosome
viruses
030106 microbiology
Mutant
Intracellular Space
lcsh:QR1-502
N-glycosylation
Endocytosis
Article
lcsh:Microbiology
EIAV
03 medical and health sciences
chemistry.chemical_compound
N-linked glycosylation
Virology
Animals
Humans
Horses
Virus Release
traffic
LAMP1
Bone Marrow Stromal Antigen 2
tetherin
Subcellular localization
Cell biology
carbohydrates (lipids)
Protein Transport
HEK293 Cells
030104 developmental biology
Infectious Diseases
antiviral function
chemistry
Mutation
Tetherin
Subjects
Details
- Language :
- English
- ISSN :
- 19994915
- Database :
- OpenAIRE
- Journal :
- Viruses
- Accession number :
- edsair.doi.dedup.....62a87eaea62e56792d78c39c49f67164
- Full Text :
- https://doi.org/10.3390/v12020220