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PGLYRP-1 mediated intracellular peptidoglycan detection promotes mucosal protection

ABSTRACT: PGLYRP-1 mediated intracellular peptidoglycan detection promotes mucosal protection

PROVIDER: PRJNA1173729 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR31016500_1.fastq.gz	Fastqsanger.gz
	SRR31016500_2.fastq.gz	Fastqsanger.gz
	SRR31016501_1.fastq.gz	Fastqsanger.gz
	SRR31016501_2.fastq.gz	Fastqsanger.gz
	SRR31016502_1.fastq.gz	Fastqsanger.gz

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PGLYRP-1 mediated intracellular peptidoglycan detection promotes mucosal protection

Project description:We identified PGLYRP-1 as a receptor for the disaccharide motif of lysine N-acetylglucosamine N-acetylmuramic tripeptide (GMTriP-K) with a newly constructed PGN microarray. Surprisingly, PGLYRP-1 was required for innate immune activation of macrophages by GMTriP-K but not N-acetylglucosamine N-acetylmuramic dipeptide (GMDiP) or muramyl dipeptide (MDP). In macrophages, intracellular PGLYRP-1 complexed with NOD2 and GEF-H1, both of which were required for GMTriP-K-regulated gene expression. PGLYRP-1 localized to the endoplasmic reticulum and interacted at the Golgi with NOD2 upon GMTriP-K stimulation. PGLYRP-1 upregulation and its dependent gene expression signatures were induced in both mouse intestinal inflammation and human ulcerative colitis. Importantly, PGLYRP-1 activation by GMTriP-K resulted in innate immune activation and protection of mice from colitis.

2025-01-31 | GSE279626 | GEO

PGLYRP1-mediated intracellular peptidoglycan detection promotes intestinal mucosal protection.

Project description:Peptidoglycan recognition proteins (PGLYRPs) are implicated in the control of the intestinal microbiota; however, molecular requirements for peptidoglycan (PGN) binding and receptor signaling mechanisms remain poorly understood. Here we show that PGLYRP1 is a receptor for the disaccharide motif of lysine N-acetylglucosamine N-acetylmuramic tripeptide (GMTriP-K). PGLYRP1 is required for innate immune activation by GMTriP-K but not muramyl dipeptide (MDP). In macrophages, intracellular PGLYRP1 complexes with NOD2 and GEF-H1, both of which are required for GMTriP-K-regulated gene expression. PGLYRP1 localizes to the endoplasmic reticulum and interacts at the Golgi with NOD2 upon GMTriP-K stimulation. PGLYRP1 and dependent gene expression signatures are induced in both mouse intestinal inflammation and human ulcerative colitis. Importantly, PGLYRP1 activation by GMTriP-K can result in the protection of mice from TNBS-induced colitis. Mammalian PGLYRPs can function as intracellular pattern recognition receptors for the control of host defense responses in the intestine.

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Mucosal Boosting Enhances Vaccine Protection Against SARS-CoV-2 in Rhesus Macaques

Project description:A major limitation of current SARS-CoV-2 vaccines is that they provide minimal protection against acquisition of infection with current Omicron subvariants, although they still provide protection against severe disease. It has been hypothesized that enhanced mucosal immunity will be required to block infection and onward transmission. Intranasal administration of current vaccines has proven inconsistent, suggesting that alternative immunization strategies may be required. Here we show that intratracheal boosting with a bivalent Ad26 based SARS-CoV-2 vaccine results in substantial induction of mucosal humoral and cellular immunity and near complete protection against SARS-CoV-2 BQ.1.1 challenge.

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Project description:CD11b+ CD11c- cells were isolated by cell sorting from the spleens of NOD and NOD.Idd3 mice. Cells were then either unstimulated or stimulated with peptidoglycan (5ug/ml) for 4 hours at 37 degrees prior to RNA extraction. Peptidoglycan was chosen as a stimulus due to its know ability to stimulate CD11b+ cells through Toll-like receptor 2 and our previous data showing biological differences between NOD and NOD.Idd3-derived CD11b+CD11c- cells after stimulation with peptidoglycan. CD11b+ cells from NOD and NOD.Idd3 were either unstimulated or stimulated with peptidoglycan(PGN) for 4 hours at 37 degerees prior to RNA extraction.

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Response of Vibrio cholerae to exogenous peptidoglycan

Project description:Using transcriptomics, we studied the transcriptional response of Vibrio cholerae to 10 min of exogenously supplied peptidoglycan at 300 µg/mL.

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Project description:Amorphous magnesium-substituted calcium phosphate (AMCP) nanoparticles form constitutively in large numbers in the gastrointestinal tract. Collective evidence indicates that they trap luminal macromolecules, such as bacterial and dietary protein antigen, delivering this cargo to mucosal antigen presenting cells. Here using a precise synthetic mimetic of the AMCP nanomineral, we studied whether trapping of macromolecules by AMCP modulates signalling of the macromolecule itself. Based upon whole genome transcriptomic analyses and using peptidoglycan as a macromolecule, we showed that neither AMCP nanomineral itself regulated any gene, nor did it modify any gene regulation by peptidoglycan. We conclude that synthetic AMCP nanomineral can deliver macromolecular cargo intracellularly without affecting gene transcription.

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Expression data from peptidoglycan stimulated CD11b+ cells from NOD and NOD.Idd3

2010-09-28 | GSE24350 | GEO