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BST-2糖基化位点的突变导致其在细胞内CD63阳性囊泡中积累，而不影响其对靶向多囊泡体的HIV-1和乙型肝炎病毒的抗病毒活性。

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.

作者信息

Han Zhu, Lv Mingyu, Shi Ying, Yu Jinghua, Niu Junqi, Yu Xiao-Fang, Zhang Wenyan

机构信息

Institute of Virology and AIDS Research, First Hospital of Jilin University, Changchun 130021, China.

Department of Hepatology, First Hospital of Jilin University, Changchun 130021, China.

出版信息

Viruses. 2016 Feb 29;8(3):62. doi: 10.3390/v8030062.

DOI:10.3390/v8030062
PMID:26938549
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC4810252/
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.

摘要

BST-2/束缚素通过“物理束缚”模型阻断包括HIV-1在内的多种包膜病毒的释放。N-连接糖基化对该模型的具体作用存在争议。在此，我们证实糖基化位点的突变产生了翻译后错误运输的效应，导致BST-2在细胞内CD63阳性囊泡中积累。具有这种表型的BST-2有效抑制了多泡体靶向的HIV-1和乙型肝炎病毒的释放，而不影响BST-2与早期内体抗原1（EEA1）和溶酶体相关膜蛋白1（LAMP1）的共定位。这些结果表明，人BST-2的N-连接糖基化对于细胞内病毒体的保留是可有可无的，这意味着这种最近发现的细胞内束缚功能可能在进化上与BST-2在细胞表面束缚新生病毒体的经典抗病毒功能不同。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/de9632ed9566/viruses-08-00062-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/ca69c2a3ed75/viruses-08-00062-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/934277fd7261/viruses-08-00062-g002a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/93ade2b8b8b5/viruses-08-00062-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/288e72c2f35d/viruses-08-00062-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/1894b8964dab/viruses-08-00062-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/de9632ed9566/viruses-08-00062-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/ca69c2a3ed75/viruses-08-00062-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/934277fd7261/viruses-08-00062-g002a.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/93ade2b8b8b5/viruses-08-00062-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/288e72c2f35d/viruses-08-00062-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/1894b8964dab/viruses-08-00062-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/ff43/4810252/de9632ed9566/viruses-08-00062-g006.jpg

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