Unveiling non-classical glycosylation patterns in Bombyx mori nucleopolyhedrovirus GP64: Insights into viral entry and fusion

文献类型： 外文期刊

第一作者： Xu, Ying

作者： Xu, Ying;Hao, Yufeng;Zhou, Tingting;Gyawu, Stephen Baffour;Sun, Luping;Pan, Shijia;Wang, Meixian;Lu, Yujie;Hao, Bifang;Huang, Jinshan;Zhou, Tingting;Wang, Meixian;Hao, Bifang;Huang, Jinshan;Lu, Yujie

作者机构：

关键词： Baculovirus; N-Glycosylation; Signal peptide; GP64; Non-classical pattern; Membrane fusion

期刊名称：VIROLOGY （ 影响因子：2.4； 五年影响因子：2.5 ）

ISSN： 0042-6822

年卷期： 2024 年 597 卷

页码：

收录情况： SCI

摘要： The glycoprotein GP64 of alphabaculovirus is crucial for viral entry and fusion. Here, we investigated the Nglycosylation patterns of Bombyx mori nucleopolyhedrovirus (BmNPV) GP64 and its signal peptide (SP) cleaved form, SP Delta nGP64, along with their impacts on viral infectivity and fusogenicity. Through deglycosylation assays, we confirmed N-glycosylation of BmNPV GP64 on multiple sites. Mutational analysis targeting predicted Nglycosylation sites revealed diverse effects on viral infectivity and cell fusion. Particularly noteworthy were mutations at sites 175, which resulted in complete loss of infectivity and fusion capacity. Furthermore, LC-MS/ MS analysis uncovered unexpected non-classical N-glycosylation sites, including N252, N302, N367, and N471, with only N302 and N471 identified in SP Delta nGP64. Subsequent investigation highlighted the critical roles of these residues in BmNPV amplification and fusion, underscoring the essentiality of N367 glycosylation for GP64 fusogenicity. Our findings provide valuable insights into the non-classical glycosylation landscape of BmNPV GP64 and its functional significance in viral biology.

分类号：

  • 相关文献
作者其他论文 更多>>

微信小程序