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Transcriptomic profiles of Pseudomonas aeruginosa PA14 grown in the presence or absence of mucins or mucin-glycans

ABSTRACT: Transcriptomic profiles of Pseudomonas aeruginosa PA14 grown in the presence or absence of mucins or mucin-glycans

PROVIDER: PRJNA659742 | ENA |

REPOSITORIES: ENA

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			Action	DRS
	SRR12534560.fastq.gz	Fastqsanger.gz
	SRR12534561.fastq.gz	Fastqsanger.gz
	SRR12534562.fastq.gz	Fastqsanger.gz
	SRR12534563.fastq.gz	Fastqsanger.gz
	SRR12534564.fastq.gz	Fastqsanger.gz

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Transcriptomic profiles of Pseudomonas aeruginosa PA14 grown in the presence or absence of mucins or mucin-glycans

Project description:We use high-throughput sequencing to profile the response of the opportunistic mucosal pathogen Pseudomonas aeruginosa to mucins and mucin-glycans from the mucosal niche. We find that P. aeruginosa undergoes a genome-wide phenotypic shift in response to mucins and their attached glycans. Specifically, nearly all virulence pathways are downregulated in response to these host-produced factors. This study provides a framework for understanding how the host environment regulates bacterial function.

2020-08-28 | GSE156995 | GEO

Transcriptomic profiles of Streptococcus mutans UA159 grown in the presence or absence of mucins or mucin glycans

Project description:We use high-throughput sequencing to profile the response of oral commensal pathogen Streptococcus mutans to mucins protein polymers (human MUC5B mucins) and soluble mucin glycans (human MUC5B glycans and porcine MUC5AC glycans). We find that mucins and their glycans alter the regulation of dozens of S. mutans genes, specifically downregulating competence-associated quorum sensing genes. The transcriptional responses induced by MUC5B mucins, MUC5B glycans, and MUC5AC glycans are highly correlated.

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Project description:We use high-throughput sequencing to profile the response of the opportunistic fungal pathogen Candida albicans to mucins and mucin-glycans from the mucosal niche. We find that C. albicans undergoes a genome-wide phenotypic shift in response to mucins and their attached glycans suppressing virulence-associated pathways.

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Transcriptomic profiles of Streptococcus mutans UA159 grown in the presence or absence of mucins or mucin glycans

Project description:Transcriptomic profiles of Streptococcus mutans UA159 grown in the presence or absence of mucins or mucin glycans

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Transcriptomic profiles of Pseudomonas aeruginosa PAO1 grown in the presence or absence of mucins or mucin-glycans

Project description:Transcriptomic profiles of Pseudomonas aeruginosa PAO1 grown in the presence or absence of mucins or mucin-glycans

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RNA-seq of human gut Bacteroides xylanisolvens and Bacteroides ovatus isolates grown on mucin O-linked glycans compared to glucose

Project description:Purpose: Examining the transcriptome of human gut bacteria (Bacteroides xylanisolvens/Bacteroides ovatus) that grow on mucin O-linked glycans as a sole carbon source Methods: Strains were grown on 10 mg/ml mucin O-linked glycans (MOG) or 5 mg/ml glucose as a sole carbon source in vitro. Fold change was calculated as MOG over glucose. Once cells reached an optical density corresponding to mid-log phase growth, RNA was isolated and rRNA depleted. Samples were multiplexed for sequencing on the Illumina HiSeq platform at the University of Michigan Sequencing Core. Data was analyzed using Arraystar software (DNASTAR, Inc.) Genes with significant up- or down-regulation were determined by the following criteria: genes with an average fold-change >10-fold and biological replicates with a normalized expression level >1% of the overall average RPKM expression level. Results: We identified genes activated in response to mucin O-linked glycans from Bacteroides xylanisolvens/Bacteroides ovatus strains

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Ruminococcus torques is a keystone degrader of intestinal mucin glycoprotein, releasing oligosaccharides used by Bacteroides thetaiotaomicron

Project description:Symbiotic interactions between humans and our communities of resident gut microbes (microbiota) play many roles in health and disease. Some gut bacteria utilize mucus as a nutrient source and can under certain conditions damage the protective barrier it forms, increasing disease susceptibility. We investigated how Ruminococcus torques—a known mucin-degrader that remains poorly studied despite its implication in inflammatory bowel diseases (IBDs)— degrades mucin glycoproteins or their component O-linked glycans to understand its effects on the availability of mucin-derived nutrients for other bacteria. We found that R. torques utilizes both mucin glycoproteins and released oligosaccharides from gastric and colonic mucins, degrading these substrates with a panoply of mostly constitutively expressed, secreted enzymes. Investigation of mucin oligosaccharide degradation by R. torques revealed strong fucosidase, sialidase and b1,4-galactosidase activities. There was a lack of detectable sulfatase and weak β1,3-galactosidase degradation, resulting in accumulation of glycans containing these structures on mucin polypeptides. While the Gram-negative symbiont, Bacteroides thetaiotaomicron grows poorly on mucin glycoproteins, we demonstrate a clear ability of R. torques to liberate products from mucins, making them accessible to B. thetaiotaomicron. This work underscores the diversity of mucin-degrading mechanisms in different bacterial species and the probability that some species are contingent on others for the ability to more fully access mucin-derived nutrients. The ability of R. torques to directly degrade a variety of mucin and mucin glycan structures and unlock released glycans for other species suggests that it is a keystone mucin degrader, which may contribute to its association with IBD.

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Ion Mobility-Tandem Mass Spectrometry of Mucin-type O-Glycans

Project description:The dense O-glycosylation of mucins plays an important role in the defensive properties of the mucus hydrogel. Aberrant glycosylation is often correlated with inflammation and pathology such as COPD, cancer, and Crohn’s disease. The inherent complexity of glycans and the diversity in the O-core structure constitute fundamental challenges for the analysis of mucin-type O-glycans. Due to coexistence of multiple isomers, multidimensional workflows such as LC-MS are required. To separate the highly polar carbohydrates, porous graphitized carbon is often used as a stationary phase. However, LC-MS workflows are time-consuming and lack reproducibility. Here we present a rapid alternative for separating and identifying O-glycans released from mucins based on trapped ion mobility mass spectrometry. Compared to established LC-MS, the acquisition time is reduced from an hour to two minutes. To test the validity, the developed workflow was applied to sputum samples from cystic fibrosis patients to map O-glycosylation features associated with disease.

2024-03-19 | PXD050530 | Pride

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