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Refined Candidate Region for F4ab/ac Susceptibility situated proximal to MUC13 in Pigs

ABSTRACT: A GWAS study was then performed in 52 non-adhesive and 68 strong adhesive pigs for F4ab/ac ETEC originating from 5 Belgian farms. A new refined candidate region (chr13: 144,810,100-144,993,222) for F4ac ETEC susceptibility was identified with MUC13 adjacent to the distal part of the region.

ORGANISM(S): Sus scrofa

PROVIDER: GSE57981 | GEO | 2014/07/31

SECONDARY ACCESSION(S): PRJNA248648

REPOSITORIES: GEO

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Refined Candidate Region for F4ab/ac Susceptibility situated proximal to MUC13 in Pigs

Project description:A GWAS study was then performed in 52 non-adhesive and 68 strong adhesive pigs for F4ab/ac ETEC originating from 5 Belgian farms. A new refined candidate region (chr13: 144,810,100-144,993,222) for F4ac ETEC susceptibility was identified with MUC13 adjacent to the distal part of the region. All pigs were phenotyped for the presence of the F4ab/ac receptor (F4ab/acR) using the in vitro villous adhesion assay with 4×108 F4ac E. coli (strain GIS26, serotype O149:K91, F4ac+) or F4ab E. coli (strain G7, serotype O8:K87, F4ab+) . A total of 120 F4ab/acR phenotyped pigs were genotyped using the Porcine SNP60 BeadChip (Illumina) containing 62,163 SNPs, according to the manufacturer’s protocol. The position of the SNPs was based on the current pig genome assembly (Sscrofa10.2).

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Refined candidate region for F4ab/ac enterotoxigenic Escherichia coli susceptibility situated proximal to MUC13 in pigs.

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MeDIP-chip for porcine intestinal epithelial cells with ETEC F4ab/ac infection

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Glycosylation Orchestrates Megakaryocytic Fate of Hematopoietic Stem Cells via Wnt-Muc13 Signaling [scMultiome]

Project description:Hematopoietic stem and progenitor cells (HSPCs) sustain blood production through tightly regulated fate decisions. Disruption of this control underlies disorders such as myelodysplastic syndromes, myeloproliferative neoplasms, and inherited thrombocytopenias. While transcriptional and epigenetic regulation of HSPCs is well established, the contribution of glycosylation has remained largely unexplored. Here, we identify the glycosyltransferase B4GALT1 as a central regulator of hematopoiesis that integrates extrinsic niche cues with intrinsic transcriptional programs. B4GALT1 shapes the bone marrow microenvironment by generating complex glycan niches that support HSPC function. However, its deficiency produces oncogenic glycan signatures, disrupts HSPC niche integrity, and induces aberrant expression of Mucin 13 (MUC13). These changes expand stem and progenitor pools, enforce megakaryocyte lineage bias, and activate the Wnt–MUC13/β-catenin signaling axis, a pathway tightly linked to proliferation and malignant transformation. Consequently, B4GALT1 loss uncouples proliferation from self-renewal, altering key regulators of stem cell quiescence, lineage balance, and marrow homeostasis. Our findings define a previously unrecognized glycan-dependent regulatory axis that directs HSPC fate through coordinated transcriptional reprogramming, signaling modulation, and niche remodeling. This work establishes aberrant glycosylation as a driver of hematopoietic dysfunction and highlights B4GALT1 as a potential therapeutic target in stem cell–driven blood disorders.

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MUC13-associated molecular interactome in pancreatic cancer

Project description:MUC13 has emerged as a critical molecular player that is involved in tumorigenesis, cancer progression, metastasis and evade immune surveillance, including in pancreatic cancer. In this report, we have identified MUC13 molecular interactome using an integrated immunoprecipitation and liquid chromatography mass spectrometry (IP-LCMS) technique and systems network biology approach to determine its functional protein-protein interaction network and its associated oncogenic mechanisms. This study reveals total 54 key interactor proteins (CDK1, CTNND1, Caludin-1, ErbB3-binding protein 1, Basic transcription factor 3 and Tight junction protein 1 protein etc) of MUC13. Interestingly majority of the interacting proteins were found to be associated with oncogenic and immune checkpoint pathways. These proteins are involved in the regulation of PD1/PD-L1, T-cell receptor signaling, and post-translational protein processing and modifications in the endoplasmic reticulum. This study also revealed that MUC13 might be involved in other cellular processes such as apoptosis, autophagy, senescence, calcium signaling, microRNA activity, lysosomal function, and diabetic cardiomyopathy. Taken together, this study for the first time elucidated MUC13 associated molecular interactome that might be involved in pancreatic cancer progression and metastasis. This study will help to develop new strategies to intervene pancreatic cancer progression via disrupting MUC13 associated oncogenic molecular network.

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Sus scrofa

Project description:Refined Candidate Region for F4ab/ac Susceptibility situated proximal to MUC13 in Pigs

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Degradation of the intestinal mucus layer by the ETEC protease EatA is species specific determined by the structure of the MUC2 mucin

Project description:Enterotoxigenic Escherichia coli (ETEC) infections are a leading cause of diarrheal illness, responsible for an estimated 100,000 deaths annually. ETEC pathogenesis is driven by various virulence factors, including toxins, adhesins, and noncanonical factors such as the protease EatA. The first line of host defense against intestinal pathogenic bacterial infections is the protective intestinal mucus layer. Here, we demonstrate the mechanism by which EatA facilitates access to the epithelial cell surface by degrading the core mucus component MUC2, thereby aiding to the infection. We identify the specific cleavage site region localized at the C-terminal of MUC2. EatA's protease activity depends on the interaction between two distinct domains, which are uniquely spaced in human MUC2, contributing to species specificity. This was confirmed using a novel chimeric mouse model solely expressing human MUC2, which allowed us to study the role of the mucus layer in the infection of human intestinal pathogens. These findings highlight how ETEC has adapted to specifically degrade the mucus layer of its human host.

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