The N-glycosylation of Equine Tetherin Affects Antiviral Activity by Regulating Its Subcellular Localization

文献类型： 外文期刊

第一作者： Bai, Bowen

作者： Bai, Bowen;Wang, Xue-Feng;Zhang, Mengmeng;Na, Lei;Zhang, Xiangmin;Zhang, Haili;Wang, Xiaojun;Wang, Xue-Feng;Yang, Zhibiao

作者机构：

关键词： tetherin; EIAV; N-glycosylation; antiviral function; traffic

期刊名称：VIRUSES-BASEL （ 影响因子：5.048； 五年影响因子：5.127 ）

ISSN：

年卷期： 2020 年 12 卷 2 期

页码：

收录情况： SCI

摘要： Tetherin is an interferon-inducible type II transmembrane glycoprotein which inhibits the release of viruses, including retroviruses, through a "physical tethering" model. However, the role that the glycosylation of tetherin plays in its antiviral activity remains controversial. In this study, we found that mutation of N-glycosylation sites resulted in an attenuation of the antiviral activity of equine tetherin (eqTHN), as well as a reduction in the expression of eqTHN at the plasma membrane (PM). In addition, eqTHN N-glycosylation mutants colocalize obviously with ER, CD63, LAMP1 and endosomes, while WT eqTHN do not. Furthermore, we also found that N-glycosylation impacts the transport of eqTHN in the cell not by affecting the endocytosis, but rather by influencing the anterograde trafficking of the protein. These results suggest that the N-glycosylation of eqTHN is important for the antiviral activity of the protein through regulating its normal subcellular localization. This finding will enhance our understanding of the function of this important restriction factor.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序