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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MDPI AG
2016-02-01
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| Series: | Viruses |
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| Online Access: | http://www.mdpi.com/1999-4915/8/3/62 |
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| author | Zhu Han Mingyu Lv Ying Shi Jinghua Yu Junqi Niu Xiao-Fang Yu Wenyan Zhang |
| author_facet | Zhu Han Mingyu Lv Ying Shi Jinghua Yu Junqi Niu Xiao-Fang Yu Wenyan Zhang |
| author_sort | Zhu Han |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-04-12T04:48:27Z |
| format | Article |
| id | doaj.art-cd5e2dfda4bf4bb49e0b0a1d37801873 |
| institution | Directory Open Access Journal |
| issn | 1999-4915 |
| language | English |
| last_indexed | 2024-04-12T04:48:27Z |
| publishDate | 2016-02-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Viruses |
| spelling | doaj.art-cd5e2dfda4bf4bb49e0b0a1d378018732022-12-22T03:47:24ZengMDPI 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 |
| 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 |
| 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_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_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_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 |
| topic | BST-2 glycosylation HIV-1 HBV |
| url | http://www.mdpi.com/1999-4915/8/3/62 |
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