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Bombyx mori

ABSTRACT: Transcriptome analysis of BmN cells following overexpression of BmSTAT gene

PROVIDER: PRJNA278107 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR3001530_1.fastq.gz	Fastqsanger.gz
	SRR3001530_2.fastq.gz	Fastqsanger.gz
	SRR3001531_1.fastq.gz	Fastqsanger.gz
	SRR3001531_2.fastq.gz	Fastqsanger.gz
	SRR3001532_1.fastq.gz	Fastqsanger.gz

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Project description:Bombyx mori BmN cells Raw sequence reads

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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.

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Comprehensive Profiling of Lysine Acetylome in Baculovirus Infected Silkworm (Bombyx mori) Cells

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.

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Project description:Transcriptome analysis of BmNPV-infected BmN-4 cells with Bm8 mutants

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