ArticleCell communication and signaling : CCS2016
HtrA-mediated E-cadherin cleavage is limited to DegP and DegQ homologs expressed by gram-negative pathogens.
Article in Cell communication and signaling : CCS, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 45 citations in OpenAlex.
- Protease-serpin-microbiome interactions in inflammatory bowel disease: toward integrated biomarkers of gut health.Gut microbes · 2026Review
- Molecular dynamics simulation-driven focused virtual screening and experimental validation of Fisetin as an inhibitor of Helicobacter pylori HtrA protease.Molecular diversity · 2025Article
- HtrA Contributes to Biofilm Formation inMicroorganisms · 2025Article
- Heterologous Expression, Purification, and Characterization of a High-Temperature Requirement A (HtrA) Protease Homologue from Leptospira.Applied biochemistry and biotechnology · 2025Article
- Convergent mechanisms of epithelial cell structure manipulation by intestinal pathogens.PLoS pathogens · 2025Review
- Role of E-cadherin in epithelial barrier dysfunction: implications for bacterial infection, inflammation, and disease pathogenesis.Frontiers in cellular and infection microbiology · 2025Review
- Contribution of Streptococcus pseudopneumoniae and Streptococcus salivarius to vocal fold mucosal integrity and function.Disease models & mechanisms · 2024Article
- Serine protease Rv2569c facilitates transmission of Mycobacterium tuberculosis via disrupting the epithelial barrier by cleaving E-cadherin.PLoS pathogens · 2024Article
- Article
- Investigating the role of aFrontiers in oral health · 2024Article
- Identification and Characterization of an HtrA Sheddase Produced byInternational journal of molecular sciences · 2023Article
- Trimer stability of Helicobacter pylori HtrA is regulated by a natural mutation in the protease domain.Medical microbiology and immunology · 2023Article
- Gastric Epithelial Barrier Disruption, Inflammation and Oncogenic Signal Transduction by Helicobacter pylori.Current topics in microbiology and immunology · 2023Review
- Connections between Exoproteome Heterogeneity and Virulence in the Oral Pathogen Aggregatibacter actinomycetemcomitans.mSystems · 2022Article
- E-Cadherin Orthologues as Substrates for the Serine Protease High Temperature Requirement A (HtrA).Biomolecules · 2022Article
- Function, molecular mechanisms, and therapeutic potential of bacterial HtrA proteins: An evolving view.Computational and structural biotechnology journal · 2022Review
- The role played by bacterial infections in the onset and metastasis of cancer.Current research in microbial sciences · 2021Review
- Article
- Gut Serpinome: Emerging Evidence in IBD.International journal of molecular sciences · 2021Review
- A novel FRET peptide assay reveals efficient Helicobacter pylori HtrA inhibition through zinc and copper binding.Scientific reports · 2020Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundThe serine proteases HtrA/DegP secreted by the human gastrointestinal pathogens Helicobacter pylori (H. pylori) and Campylobacter jejuni (C. jejuni) cleave the mammalian cell adhesion protein E-cadherin to open intercellular adhesions. A wide range of bacteria also expresses the HtrA/DegP homologs DegQ and/or DegS, which significantly differ in structure and function.
methodsE-cadherin shedding was investigated in infection experiments with the Gram-negative pathogens H. pylori, enteropathogenic Escherichia coli (EPEC), Salmonella enterica subsp. Enterica (S. Typhimurium), Yersinia enterocolitica (Y. enterocolitica), and Proteus mirabilis (P. mirabilis), which express different combinations of HtrAs. Annotated wild-type htrA/degP, degQ and degS genes were cloned and proteolytically inactive mutants were generated by a serine-to-alanine exchange in the active center. All HtrA variants were overexpressed and purified to compare their proteolytic activities in casein zymography and in vitro E-cadherin cleavage experiments.
resultsInfection of epithelial cells resulted in a strong E-cadherin ectodomain shedding as reflected by the loss of full length E-cadherin in whole cell lysates and formation of the soluble 90 kDa extracellular domain of E-cadherin (NTF) in the supernatants of infected cells. Importantly, comparing the caseinolytic and E-cadherin cleavage activities of HtrA/DegP, DegQ and DegS proteins revealed that DegP and DegQ homologs from H. pylori, S. Typhimurium, Y. enterocolitica, EPEC and P. mirabilis, but not activated DegS, cleaved E-cadherin as a substrate in vitro.
conclusionsThese data indicate that E-cadherin cleavage is confined to HtrA/DegP and DegQ proteins representing an important prevalent step in bacterial pathogenesis.
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