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Viruses 2016, 8(3), 62; doi:10.3390/v8030062

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

1
Institute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, China
2
Department of Hepatology, First Hospital of Jilin University, Changchun 130021, China
These authors contributed equally to this work.
*
Authors to whom correspondence should be addressed.
Academic Editor: Curt Hagedorn
Received: 17 December 2015 / Revised: 12 February 2016 / Accepted: 17 February 2016 / Published: 29 February 2016
(This article belongs to the Section Antivirals & Vaccines)
View Full-Text   |   Download PDF [8430 KB, uploaded 29 February 2016]   |  

Abstract

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-trafficking, leading to an accumulation of BST-2 at intracellular CD63-positive vesicles. BST-2 with this phenotype potently inhibited the release of multivesicular body-targeted HIV-1 and hepatitis B virus, without affecting the co-localization of BST-2 with EEA1 and LAMP1. These results suggest that N-linked glycosylation of human BST-2 is dispensable for intracellular virion retention and imply that this recently discovered intracellular tethering function may be evolutionarily distinguished from the canonical antiviral function of BST-2 by tethering nascent virions at the cell surface. View Full-Text
Keywords: BST-2; glycosylation; HIV-1; HBV BST-2; glycosylation; HIV-1; HBV
This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

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MDPI and ACS Style

Han, Z.; Lv, M.; Shi, Y.; Yu, J.; Niu, J.; Yu, X.-F.; Zhang, W. 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. Viruses 2016, 8, 62.

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