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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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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spelling doaj-cd5e2dfda4bf4bb49e0b0a1d378018732020-11-24T23:40:44ZengMDPI AGViruses1999-49152016-02-01836210.3390/v8030062v8030062Mutation 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 VirusZhu Han0Mingyu Lv1Ying Shi2Jinghua Yu3Junqi Niu4Xiao-Fang Yu5Wenyan Zhang6Institute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, ChinaInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, ChinaInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, ChinaInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, ChinaDepartment of Hepatology, First Hospital of Jilin University, Changchun 130021, ChinaInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, ChinaInstitute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, ChinaBST-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.http://www.mdpi.com/1999-4915/8/3/62BST-2glycosylationHIV-1HBV
collection DOAJ
language English
format Article
sources DOAJ
author Zhu Han
Mingyu Lv
Ying Shi
Jinghua Yu
Junqi Niu
Xiao-Fang Yu
Wenyan Zhang
spellingShingle Zhu Han
Mingyu Lv
Ying Shi
Jinghua Yu
Junqi Niu
Xiao-Fang Yu
Wenyan Zhang
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
BST-2
glycosylation
HIV-1
HBV
author_facet Zhu Han
Mingyu Lv
Ying Shi
Jinghua Yu
Junqi Niu
Xiao-Fang Yu
Wenyan Zhang
author_sort Zhu Han
title 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
title_short 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
title_full 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
title_fullStr 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
title_full_unstemmed 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
title_sort 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
publisher MDPI AG
series Viruses
issn 1999-4915
publishDate 2016-02-01
description 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.
topic BST-2
glycosylation
HIV-1
HBV
url http://www.mdpi.com/1999-4915/8/3/62
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