Glycosylation of canine tetherin is essential for its antiviral activity against H3N2 canine influenza virus.

ABSTRACT: Tetherin is an interferon-induced-expressing transmembrane protein that utilizes a unique topology to restrict the release of enveloped viruses from the surface of the cell membrane. N-linked glycosylation plays an important role in protein post-translational modifications. To investigate the role of glycosylation in the antiviral activity of canine tetherin, its potential glycosylation sites were predicted and mutated, and the effects of glycosylation site mutations or treatment with a glycosylation inhibitor on the ability of canine tetherin to restrict H3N2 canine influenza virus (CIV) replication were examined. Mutations in the glycosylation sites of canine tetherin (N72A, N99A, and N72,99A) lead to changes in its intracellular distribution and weakened or even lost antiviral activity

SUBMITTER: Xu L 

PROVIDER: S-EPMC12325054 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature