Mutation of Glycosylation Sites in BST-2 Leads to Its Accumulation at Intracellular CD63-Positive Vesicles without Affecting Its Antiviral Activity against Multivesicular Body-Targeted HIV-1 and Hepatitis B Virus

Mutation of Glycosylation Sites in BST-2 Leads to Its Accumulation at Intracellular CD63-Positive Vesicles without Affecting Its Antiviral Activity against Multivesicular Body-Targeted HIV-1 and Hepatitis B Virus

BST-2/tetherin blocks the release of various enveloped viruses including HIV-1 with a “physical tethering” model. The detailed contribution of N-linked glycosylation to this model is controversial. Here, we confirmed that mutation of glycosylation sites exerted an effect of post-translational mis-tr...

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Bibliographic Details
Main Authors: Zhu Han, Mingyu Lv, Ying Shi, Jinghua Yu, Junqi Niu, Xiao-Fang Yu, Wenyan Zhang
Format: Article
Language:English
Published: MDPI AG 2016-02-01
Series:Viruses
Subjects:
BST-2
glycosylation
HIV-1
HBV
Online Access:http://www.mdpi.com/1999-4915/8/3/62

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