Proteomic characterization of host proteins interacting with wild-type and signal peptide-cleaved GP64 of Bombyx mori nucleopolyhedrovirus (BmNPV)

文献类型： 外文期刊

第一作者： Chen, Kai

作者： Chen, Kai;Li, Qilong;Wu, Shuyan;Hao, Bifang;Huang, Jinshan;Hao, Bifang;Huang, Jinshan

作者机构：

关键词： BmNPV; GP64; Envelope protein-host interaction; Proteomics; Signal peptide

期刊名称：MICROBIAL PATHOGENESIS （ 影响因子：3.5； 五年影响因子：3.6 ）

ISSN： 0882-4010

年卷期： 2025 年 208 卷

页码：

收录情况： SCI

摘要： Bombyx mori nucleopolyhedrovirus (BmNPV) relies on the envelope glycoprotein GP64 to mediate host cell entry. Both the wild-type GP64 (retaining its signal peptide, SP) and the SP-cleaved variant (SP Delta nGP64) can mediate viral entry. However, their mechanisms may differ. To identify potential GP64 receptors and dissect host interaction profiles, we performed comparative co-immunoprecipitation using purified GP64 and SP Delta nGP64, followed by data-independent acquisition (DIA)-based proteomic analysis. A total of 6064 and 5247 host proteins were identified, respectively. Enrichment analyses revealed shared involvement in membrane trafficking, lipid metabolism, and endocytosis-pathways essential for viral entry. Four candidate host proteins-SCARB4, TMED10, PLEKHF2, and EXOC2-were prioritized based on membrane localization and functional relevance. Temporal expression analysis showed early transcriptional induction during infection. Functional assays demonstrated that RNAi knockdown of these genes significantly reduced infection efficiency, while overexpression promoted viral infection, particularly for SP Delta nGP64-expressing virions. These results suggest that both GP64 variants exploit overlapping host pathways, yet may differ in receptor usage or entry dynamics. This study establishes a comparative interactome framework for wild-type and SP-cleaved GP64, providing new insights into BmNPV infection mechanisms and aiding in the identification of potential GP64 receptors for future antiviral interventions.

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