Dataset Information

Protein (elafin) cleavage by the main Lactobacillus spp encountered in the female gynecological tract

ABSTRACT: Mass spectrometry analyses for determining whether 13C615N2-labeled lysines contained in the elafin (innate peptide highly expressed in lower female genital tract and down-regulated in case of HPV infection) were found in the amino acid sequence of some proteins of Lactobacilli, supporting the fundamental role of innate secretion in the growth/survival of acid lactic bacteria (L. crispatus, L. jensenii and L. iners).

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Lactobacillus

SUBMITTER: Dominique Baiwir

LAB HEAD: Michael Herfs

PROVIDER: PXD022113 | Pride | 2022-04-04

REPOSITORIES: Pride

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Publications

HPV infection alters vaginal microbiome through down-regulating host mucosal innate peptides used by Lactobacilli as amino acid sources.

Lebeau Alizee A Bruyere Diane D Roncarati Patrick P Peixoto Paul P Hervouet Eric E Cobraiville Gael G Taminiau Bernard B Masson Murielle M Gallego Carmen C Mazzucchelli Gabriel G Smargiasso Nicolas N Fleron Maximilien M Baiwir Dominique D Hendrick Elodie E Pilard Charlotte C Lerho Thomas T Reynders Celia C Ancion Marie M Greimers Roland R Twizere Jean-Claude JC Daube Georges G Schlecht-Louf Geraldine G Bachelerie Françoise F Combes Jean-Damien JD Melin Pierrette P Fillet Marianne M Delvenne Philippe P Hubert Pascale P Herfs Michael M

Nature communications 20220228 1

Despite the high prevalence of both cervico-vaginal human papillomavirus (HPV) infection and bacterial vaginosis (BV) worldwide, their causal relationship remains unclear. While BV has been presumed to be a risk factor for HPV acquisition and related carcinogenesis for a long time, here, supported by both a large retrospective follow-up study (n = 6,085) and extensive in vivo data using the K14-HPV16 transgenic mouse model, we report a novel blueprint in which the opposite association also exist ...[more]

PMID: 35228537

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Project description:The genome-wide analysis of the binding sites of the transcription factor vitamin D receptor (VDR) is essential for a global appreciation the physiological impact of the nuclear hormone 1M-NM-1,25-dihydroxyvitamin D3 (1,25(OH)2D3). Genome-wide analysis of lipopolysaccharide (LPS)-polarized THP-1 human monocytic leukemia cells via chromatin immunoprecipitation (ChIP) coupled with massive parallel sequencing (ChIP-seq) resulted in 1,318 high-confidence VDR binding sites, of which 789 and 364 occurred uniquely with and without 1,25(OH)2D3 stimulation, while only 165 were common. We re-analyzed five public VDR ChIP-seq datasets with identical peak calling settings (MACS, version 2) and found in total 23,409 non-overlapping VDR binding sites, 75% of which are unique within the six analyzed cellular models. LPS-differentiated THP-1 cells have 22% more genomic VDR locations than undifferentiated cells and both cell types display more overlap in their VDR locations than the other investigated cell types. In general, the intersection of VDR binding profiles of ligand-stimulated cells is higher than those of unstimulated cells. De novo binding site searches and DR3-type binding site screening using HOMER of the six VDR ChIP-seq datasets suggest that DR3 sites are strongly associated with the ligand-responsiveness of VDR occupation. Importantly, all VDR ChIP-seq datasets display the same relationship between the VDR occupancy and the percentage of DR3-type sequences below the peak summits. The comparative analysis of six VDR ChIP-seq datasets demonstrated that the mechanistic basis for the action of the VDR is independent of the cell type. Only the minority of genome-wide VDR binding sites contains a DR3-type sequence. Moreover, the total number of identified VDR binding sites in each ligand-stimulated cell line inversely correlates with the percentage of peak summits with DR3 sites. Systematic reanalysis of 5 published VDR ChIP-seq datasets together with a new dataset from 24 h LPS-treated THP-1 cells at the unstimulated state and after 80 min ligand (10 nM 1M-NM-1,25(OH)2D3 (1,25D, calcitriol)) treatment. See GSM1280896 and GSM1280896 Sample records for data processing information. GSE53041_README.txt has additional details.

Dataset Information

Protein (elafin) cleavage by the main Lactobacillus spp encountered in the female gynecological tract

Publications

HPV infection alters vaginal microbiome through down-regulating host mucosal innate peptides used by Lactobacilli as amino acid sources.

Similar Datasets

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