The N-glycosylation of Equine Tetherin Affects Antiviral Activity by Regulating Its Subcellular Localization.
EIAV
N-glycosylation
antiviral function
tetherin
traffic
Journal
Viruses
ISSN: 1999-4915
Titre abrégé: Viruses
Pays: Switzerland
ID NLM: 101509722
Informations de publication
Date de publication:
16 02 2020
16 02 2020
Historique:
received:
11
12
2019
revised:
28
01
2020
accepted:
12
02
2020
entrez:
22
2
2020
pubmed:
23
2
2020
medline:
20
2
2021
Statut:
epublish
Résumé
Tetherin is an interferon-inducible type II transmembrane glycoprotein which inhibits the release of viruses, including retroviruses, through a "physical tethering" 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.
Identifiants
pubmed: 32079099
pii: v12020220
doi: 10.3390/v12020220
pmc: PMC7077275
pii:
doi:
Substances chimiques
Bone Marrow Stromal Antigen 2
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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