Ontology highlight
ABSTRACT:
PROVIDER: PRJNA792944 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR17373631.fastq.gz | Fastqsanger.gz | |||
| SRR17373632.fastq.gz | Fastqsanger.gz | |||
| SRR17373633.fastq.gz | Fastqsanger.gz | |||
| SRR17373634.fastq.gz | Fastqsanger.gz | |||
| SRR17373635.fastq.gz | Fastqsanger.gz |
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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.
2017-11-27 | PXD008054 | Pride
Project description:<p>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.</p>
2025-12-03 | MTBLS13447 | MetaboLights
Project description:As important roles of small RNA pathways, AGO proteins mediate interaction of incorporated small RNAs with their targets. The resolution of AGO associated small RNAs showed a significant landscape of AGO proteins and their binding small RNAs. To characterize small RNAs that associated with BmAGO2 protein in Bombyx mori, the small RNA population associated with BmAGO2 in BmN cells was extracted from the AGO immunoprecipitated complex and the small RNAs between 17nt to 50nt separated by a polyacrylamide gel electrophoresis were subjected to library construction and deep sequencing.The high throughput sequencing yielded a total of 11691441 reads, representing 813,702 unique reads with a abundance from 5731905 to 1. Small RNA associated with AGO2 of BmN cell infected with ie1-bacmid recombinant viruses were performed by high-throughput using Hiseq 2000.
2013-03-05 | E-GEOD-41841 | biostudies-arrayexpress
Project description:Transcriptome analysis of BmNPV-infected BmN-4 cells with Bm8 mutants
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Project description:Transcriptome and epigenomic analyses of BmN-4 cells infected with BmNPV
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Project description:Employed BmN cell after 10 MOI (multiplicity of infection) BmNPV 36 hpi (hour post-infection) to compare the proteomics by LC-MS/MS
2018-05-22 | PXD008856 | Pride
Project description:RNA-seq of BmNPV cells infected by indicated mutant BmNPV to determine the impact on viral gene expression of the cis-interacting sites on BmNPV by knocking out them via RED system
2024-10-01 | GSE278147 | GEO