Apolipophorin-III modulates antiviral defense in Bombyx mori: an integrated transcriptomic and lipidomic analysis of its inhibitory role against BmNPV infection.

ABSTRACT:

The silkworm (Bombyx mori) is an economically important insect and a lepidopteran model organism. Controlling viral infections is crucial for the sustainable development of sericulture. Bombyx mori nucleopolyhedrovirus (BmNPV) infection can cause large-scale mortality in silkworm populations. Insect apolipophorin-III (ApoLp-III) has been reported to play a key role in immune recognition. Spatiotemporal expression profile analysis in this study revealed that the Bombyx mori ApoLp-III gene is highly expressed in the fat body, hemolymph, and silk gland, and its expression was significantly upregulated (p < 0.01) in BmNPV-infected fat body tissues and BmN cells. A pIZT-ApoLp-III overexpression vector was constructed, and siRNA was designed to overexpress and knock down the ApoLp-III gene in BmN cells. Following BmNPV infection, its impact on BmNPV proliferation was detected. Results showed that ApoLp-III overexpression led to a significant decrease in BmNPV genomic copy number and VP39 protein expression levels. Conversely, ApoLp-III knockdown resulted in a significant increase in BmNPV genomic copy number and VP39 protein expression. These results indicate that apolipoprotein III can inhibit BmNPV proliferation. RNA-seq analysis of the ApoLp-III overexpression stable cell line identified 451 up-regulated and 616 down-regulated genes. GO functional annotation indicated that these differentially expressed genes were significantly enriched in biological regulation, metabolic processes, and cellular components. KEGG pathway analysis showed significant enrichment of differential genes in DNA replication, cell cycle, and mismatch repair pathways. Co-immunoprecipitation screening for ApoLp-III interacting proteins identified 35 host proteins from Bombyx mori, including immune-related proteins (TR-type G domain-containing protein, immunoglobulin-like protein, etc.), transport-related proteins (talin-1, TOM1-like protein, endoplasmic reticulum membrane protein), and energy-related proteins (lipocalin, insulin-degrading enzyme), as well as 3 BmNPV-encoded proteins: viral nucleocapsid protein, BRO protein, and chitinase. In summary, these findings preliminarily suggest that the Bombyx mori ApoLp-III protein may inhibit BmNPV proliferation by participating in immune pathways or through protein-protein interactions. The underlying molecular mechanisms warrant further investigation.

INSTRUMENT(S): Liquid Chromatography MS - negative - reverse-phase, Liquid Chromatography MS - positive - reverse-phase

PROVIDER: MTBLS13447 | MetaboLights | 2025-12-03

REPOSITORIES: MetaboLights