Project description:Bombyx mori nucleopolyhedrovirus (BmNPV) relies on the envelope glycoprotein GP64 to mediate host cell entry. Intriguingly, both the wild-type GP64 retaining its signal peptide (SP) and the SP-cleaved variant (SP∆nGP64) can support viral invasion, yet their mechanisms may differ. To identify potential GP64 receptors and dissect host interaction profiles, we performed comparative co-immunoprecipitation using purified GP64 and SP∆nGP64, followed by data-independent acquisition (DIA)-based proteomic analysis. A total of 6,064 and 5,247 host proteins were identified, respectively. Enrichment analyses revealed shared involvement in membrane trafficking, lipid metabolism, and endocytosis—pathways essential for viral entry.
Project description:Bombyx mori is one of the key lepidopteran model species, and is economically important for silk production and proteinaceous drug expression. Baculovirus and insect host are important natural biological models for studying host-pathogen interactions. The impact of Bombyx mori nucleopolyhedrovirus (BmNPV) infection on the proteome and acetylome of Bombyx mori ovarian (BmN) cells were explored to facilitate a better understanding of infection-driven interactions between BmNPV and host in vitro. The proteome and acetylome were profiled through 6-plex Tandem mass tag (TMT) labelling-based quantitative proteomics. Totally, 4,194 host proteins were quantified, of which 33 were up-regulated and 47 were down-regulated in BmN cells at 36 h post-infection. Based on the proteome, quantifiable differential Kac proteins were identified and functionally annotated to gene expression regulation, energy metabolism, substance synthesis and metabolism after BmNPV infection. Altogether, 644 Kac sites in 431 host proteins and 39 Kac sites in 22 viral proteins were identified and quantified in infected BmN cells. Our study demonstrated that BmNPV infection globally impacts the proteome and acetylome of BmN cells. The viral proteins are also acetylated by the host acetyltransferase. Protein acetylation is essential for cellular self-regulation and response to virus infection. This study provides new insights for understanding the host-virus interaction mechanisms, and the role of acetylation in BmN cellular response to viral infection.