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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...
Autores principales: | Han, Zhu, Lv, Mingyu, Shi, Ying, Yu, Jinghua, Niu, Junqi, Yu, Xiao-Fang, Zhang, Wenyan |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4810252/ https://www.ncbi.nlm.nih.gov/pubmed/26938549 http://dx.doi.org/10.3390/v8030062 |
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