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The N-glycosylation of Equine Tetherin Affects Antiviral Activity by Regulating Its Subcellular Localization

Authors :
Xiangmin Zhang
Haili Zhang
Xiaojun Wang
Bowen Bai
Xue-Feng Wang
Mengmeng Zhang
Zhibiao Yang
Lei Na
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.

Details

Language :
English
ISSN :
19994915
Database :
OpenAIRE
Journal :
Viruses
Accession number :
edsair.doi.dedup.....62a87eaea62e56792d78c39c49f67164
Full Text :
https://doi.org/10.3390/v12020220