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Transcription of bovine milk and meat factors (BMMFs) in HEK293TT cells

ABSTRACT: Transcription of bovine milk and meat factors (BMMFs) in HEK293TT cells

OTHER RELATED OMICS DATASETS IN: GSE98192

PROVIDER: PRJNA384223 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR5480990_1.fastq.gz	Fastqsanger.gz
	SRR5480990_2.fastq.gz	Fastqsanger.gz
	SRR5481000_1.fastq.gz	Fastqsanger.gz
	SRR5481000_2.fastq.gz	Fastqsanger.gz
	SRR5481010_1.fastq.gz	Fastqsanger.gz

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Transcription of bovine milk and meat factors (BMMFs) in HEK293TT cells

Project description:We analyze the transcription of these bovine milk and meat factors (BMMFs) and MS isolates in human HEK293TT cells. While all analyzed DNA agents are readily transcribed, one of the MS brain isolates (MSBI1.176), sharing homology with a transmissible spongiform encephalopathy (TSE)-associated DNA molecule, is transcribed at highest levels. Our results support the transcription of an open reading frame (ORF) encoding a replication-associated protein, which is highly conserved among all isolated BMMFs. In the case of the cow milk isolate CMI1.252, transcription also occurs in a second large ORF. Transcriptome profiling upon BMMF expression identified host cellular gene expression changes related to cell cycle progression and cell viability control, indicating potential pathways for a pathogenic involvement of BMMFs.

2018-02-05 | GSE98192 | GEO

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Project description:Here we studied the glycation of bovine milk proteins by lactose as dominant sugar in milk and hexoses using tandem mass spectrometry (CID and ETD mode). In a bottom-up proteomics approach after enriching glycated peptides by boronate affinity chromatography, first we could identify 260 lactosylated peptides corresponding to 124 lactosylation sites in 28 bovine milk proteins in raw milk, raw colostrum, three brands of pasteurized milk, three brands of UHT milk, and five brands of infant formula. The same regular and additionally two lactose-free milk products (pasteurized and UHT milk) where lactose is enzymatically cleaved into the more reactive hexoses were analyzed in terms of hexosylation sites that resulted in identification of 124 hexosylated tryptic peptides corresponding to 86 glycation sites in 17 bovine milk proteins. In quantitative terms glycation increased from raw milk to pasteurized milk to UHT milk and infant formula, i.e., with the harsher processing conditions. Lactose-free milk contained significantly higher hexosylation degrees than the corresponding regular milk product.

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