Role of sulfated glycans on intestinal mucins
Ontology highlight
ABSTRACT:
PROVIDER: PRJEB62759 | ENA |
REPOSITORIES: ENA
Similar Datasets
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.
2021-01-01 | GSE163258 | GEO
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.
2019-10-20 | GSE136097 | GEO
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
Project description:A site-specific description of a recently discovered HexNAc-sulfated N-glycans of human immunoglobulin A (IgA) was still pending. Here we provide an in-depth N-glycoproteomic analysis of human serum IgA. This in-depth N-glycoproteomic analysis, developed by us, integrates a new strategy for identifying sulfated and other rare N-glycans in IgA. In our study, we implemented two strategies for identifying the new N-glycan compositions: screening for rare glycopeptides using oxonium marker ions and wildcard search to identify glycans holding a rare modification attached to peptides. The dataset provided here contains primarily IgA N-glycopeptides identified from technical quadruplicates of two commercial human serum IgA samples. A comparison of the N-glycosylation profiles of two commercial human serum IgA samples demonstrated that sulfated N-glycans are mainly present in the tailpiece site. Also, complex-type N-glycan compositions with O-acetylated sialic acid were identified in the tailpiece. Surprisingly, N-glycans bearing glucuronic acid were identified in the commercial IgA samples, but from peptides of contaminant glycoproteins.These N-glycans have not been included in previously published IgA micro-heterogeneity analyses. We expect that a broader micro-heterogeneity description of clinically relevant glycoproteins, such as IgA, can expand the screening for biomarkers or treatment options.
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Project description:FGF signaling is essential for salivary gland (SG) development and heparan sulfate (HS) regulation of FGFR function is determined by immense structural diversity of sulfated HS domains. The basement membrane (BM), containing HS proteoglycans, collagens and laminins, separates epithelia from stroma and controls growth factor-matrix cross-talk. 3-O-sulfotransferases generate highly 3-O-sulfated HS domains (3-O-HS) and Hs3st3a1 and Hs3st3b1 are enriched in myoepithelial cells (MECs), which produce BM and are a growth factor signaling hub. To investigate 3-O-HS regulation of MEC function and growth factor signaling, we generated Hs3st3a1;Hs3st3b1 double knockout (DKO) mice. The DKO HS loses specific highly 3-O-sulfated tetrasaccharides, which increases FGF/FGFR-complex binding to HS. During development this leads to increased FGFR-, BM- and MEC-related gene expression. However, in adult DKO SGs the secretory units containing acinar and MECs, have reduced MECs, increased BM and disrupted acinar polarity, resulting in salivary hypofunction. We used defined 3-O-sulfated-HS in FGFR pulldown assays and primary organ cultures to investigate 3-O-HS-dependent mechanisms regulating MEC development. We find that 3-O-HS modulates FGFR signaling to regulate MEC BM synthesis which is critical for secretory unit homeostasis and acinar function. Understanding how sulfated HS regulates development will inform the use of HS mimetics in organ regeneration.
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Project description:FGF signaling is essential for salivary gland (SG) development and heparan sulfate (HS) regulation of FGFR function is determined by immense structural diversity of sulfated HS domains. The basement membrane (BM), containing HS proteoglycans, collagens and laminins, separates epithelia from stroma and controls growth factor-matrix cross-talk. 3-O-sulfotransferases generate highly 3-O-sulfated HS domains (3-O-HS) and Hs3st3a1 and Hs3st3b1 are enriched in myoepithelial cells (MECs), which produce BM and are a growth factor signaling hub. To investigate 3-O-HS regulation of MEC function and growth factor signaling, we generated Hs3st3a1;Hs3st3b1 double knockout (DKO) mice. The DKO HS loses specific highly 3-O-sulfated tetrasaccharides, which increases FGF/FGFR-complex binding to HS. During development this leads to increased FGFR-, BM- and MEC-related gene expression. However, in adult DKO SGs the secretory units containing acinar and MECs, have reduced MECs, increased BM and disrupted acinar polarity, resulting in salivary hypofunction. We used defined 3-O-sulfated-HS in FGFR pulldown assays and primary organ cultures to investigate 3-O-HS-dependent mechanisms regulating MEC development. We find that 3-O-HS modulates FGFR signaling to regulate MEC BM synthesis which is critical for secretory unit homeostasis and acinar function. Understanding how sulfated HS regulates development will inform the use of HS mimetics in organ regeneration.
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Project description:1. NanoLC-MS2-pd-MS3 dataset on permethylated sulfated AGS O-Glycans
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2017-06-19 | MSV000081172 | GNPS
Project description:Dr. Schwarting's research is focused on the analysis of developmentally regulated cell surface molecules and their role in axon guidance and neuronal migration, using the olfactory system as a model. The interaction of cell surface glycans with endogenous lectins in the extracellular matrix provides one mechanism by which axons can utilize specific pathways as they grow towards their targets. We have a mutant mouse (b3GNT2 KO) that up-regulates the expression of lactosamine containing glycans in a subset of olfactory neurons. Gene expression profiling was performed using control and mutant mice that up-regulate the expression of lactosamine containing glycans in a subset of olfactory neurons. Glycosyltransferase expression that differed between control and mutant mice were identified.
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Project description:1. NanoLC-MS2-pd-MS3 dataset on permethylated sulfated AGS O-Glycans
2. NanoLC-MS2-pd-MS3 dataset for the permethylated N-glycans of mouse brain striatum
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