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
复制标题
BST-2 中糖基化位点的突变导致其在细胞内 CD63 阳性囊泡中积累，但不影响其针对多囊泡体靶向 HIV-1 和乙型肝炎病毒的抗病毒活性
DOI：
10.3390/v8030062
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发表时间：
2016-03-01
期刊：
影响因子：
4.7
通讯作者：
Zhang, Wenyan
中科院分区：
文献类型：
--
作者：
Han, Zhu;Lv, Mingyu;Zhang, Wenyan
BST-2/tetherin通过“物理栓系”模型阻止包括HIV-1在内的各种包膜病毒的释放。N-连接的糖基化对该模型的详细贡献是有争议的。在这里，我们证实了糖基化位点的突变产生了翻译后错误运输的影响，导致BST-2在细胞内CD 63阳性囊泡中的积累。具有该表型的BST-2有效地抑制多泡体靶向的HIV-1和乙型肝炎B病毒的释放，而不影响BST-2与EEA 1和LAMP 1的共定位。这些结果表明，人BST-2的N-连接的糖基化是细胞内病毒体保留的关键，并暗示这种最近发现的细胞内拴系功能可以通过在细胞表面拴系新生病毒体而与BST-2的典型抗病毒功能在进化上区分开。
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.