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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Detalles Bibliográficos
Autores principales: Han, Zhu, Lv, Mingyu, Shi, Ying, Yu, Jinghua, Niu, Junqi, Yu, Xiao-Fang, Zhang, Wenyan
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2016
Materias:
Article
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

Internet

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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