Ontology highlight
ABSTRACT:
PROVIDER: PRJNA1262002 | ENA |
REPOSITORIES: ENA
Dataset's files
| Action | DRS | |||
|---|---|---|---|---|
| SRR33536512_1.fastq.gz | Fastqsanger.gz | |||
| SRR33536512_2.fastq.gz | Fastqsanger.gz | |||
| SRR33536513_1.fastq.gz | Fastqsanger.gz | |||
| SRR33536513_2.fastq.gz | Fastqsanger.gz | |||
| SRR33536514_1.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: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:Baculovirus expression systems have been widely used to produce recombinant mammalian proteins owing to the lack of viral replication in vertebrates. Although several lines of evidence have demonstrated impacts of baculovirus infection in mammalian hosts, genome-wide effects have not been fully elucidated. Here, we provide comparative transcriptome profiles of baculovirus and host-immune response genes in recombinant baculovirus-infected mammalian and insect cells. Specifically, to decipher the impacts of baculovirus infection in mammalian cells, we conducted total RNA-seq on human 293 cells and insect Sf9 cells infected with recombinant baculovirus. We found that baculovirus genes were rarely expressed under the control of baculoviral promoters in 293 cells. Although some baculovirus early genes, such as PE38 and IE-01, showed limited expression in 293 cells, baculoviral late genes were mostly silent. We also found modest induction of a small number of mammalian immune response genes associated with Toll-like receptors, cytokine signaling, and complement in baculovirus-infected 293 cells. These comprehensive transcriptome data will contribute to improving recombinant baculovirus as tools for gene delivery, gene therapy, and vaccine development.
2020-09-28 | GSE158603 | GEO
Project description:The human Adeno-Associated Virus serotype 2 (WT AAV2) is a common non-pathological virus and its recombinant form (rAAV) is widely used as gene therapy vector. However, it has been shown that WT AAV2 and recombinant AAV display significantly different characteristics, especially regarding infection rate, with a near perfect infectivity and better encapsidation rate of WT AAV2. Even though rAAVs are routinely produced in the Baculovirus/Sf9 cell system, WT AAV2 has never been produced in this context. To understand the infectivity and encapsidation rate differences between WT AAV2 and rAAV, we tried to produce WT AAV2 in baculovirus/Sf9 cells system hypothesizing that the WT AAV2 may be considered as a normal recombinant AAV transgene. Through our attempts to produce WT AAV2 in Baculovirus/Sf9, we found that WT AAV2 p5 promoter, which controls the expression of large Rep proteins in mammalian cells, was active in this system. p5 promoter activity in the baculovirus/Sf9 cell system led to the expression of Rep78 that finally excises WT AAV2 genome from the baculovirus genome during the earliest phase of baculovirus stock production. The p5 promoter expression kinetics and the specific strand RNA-Seq analysis of the WT AAV2, rAAV Rep2/Cap2 cassettes in the baculovirus context was performed. We demonstrate that the WT AAV2 native promoters, p5, p19 and p40 are all active and lead to the expression of different proteins and peptides. In addition, this study demonstrates that the baculovirus brings at least some of the helper functions needed in the AAV replication/life cycle.
2018-06-21 | GSE96855 | GEO
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:Transcriptome analysis of BmNPV-infected BmN-4 cells with Bm8 mutants
| PRJDB13017 | ENA