ArticleJournal of basic microbiology2013
The stability and activity of recombinant Helicobacter pylori HtrA under stress conditions.
Article in Journal of basic microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Molecular dynamics simulation-driven focused virtual screening and experimental validation of Fisetin as an inhibitor of Helicobacter pylori HtrA protease.Molecular diversity · 2025Article
- Heterologous Expression, Purification, and Characterization of a High-Temperature Requirement A (HtrA) Protease Homologue from Leptospira.Applied biochemistry and biotechnology · 2025Article
- The immunopathogenesis ofFrontiers in microbiology · 2024Review
- A Regulatory SRNA Rli43 Is Involved in the Modulation of Biofilm Formation and Virulence inPathogens (Basel, Switzerland) · 2022Article
- E-Cadherin Orthologues as Substrates for the Serine Protease High Temperature Requirement A (HtrA).Biomolecules · 2022Article
- Identification of Desmoglein-2 as a novel target of Helicobacter pylori HtrA in epithelial cells.Cell communication and signaling : CCS · 2021Article
- A novel FRET peptide assay reveals efficient Helicobacter pylori HtrA inhibition through zinc and copper binding.Scientific reports · 2020Article
- Chaperone activity of serine protease HtrA of Helicobacter pylori as a crucial survival factor under stress conditions.Cell communication and signaling : CCS · 2019Article
- Review
- The unique trimeric assembly of the virulence factor HtrA fromThe Journal of biological chemistry · 2019Article
- Properties of the HtrA Protease From BacteriumFrontiers in microbiology · 2019Article
- Diffuse Gastric Cancer: A Summary of Analogous Contributing Factors for Its Molecular Pathogenicity.International journal of molecular sciences · 2018Review
- Amino-Terminal Processing ofFrontiers in microbiology · 2018Article
- Review
- Identification of E-cadherin signature motifs functioning as cleavage sites for Helicobacter pylori HtrA.Scientific reports · 2016Article
- Calcium binding protects E-cadherin from cleavage by Helicobacter pylori HtrA.Gut pathogens · 2016Article
- Temperature-dependent expression of virulence genes in fish-pathogenic bacteria.Frontiers in microbiology · 2015Review
- The functional interplay of Helicobacter pylori factors with gastric epithelial cells induces a multi-step process in pathogenesis.Cell communication and signaling : CCS · 2013Review
- Borrelia burgdorferi aggrecanase activity: more evidence for persistent infection in Lyme disease.Frontiers in cellular and infection microbiology · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 2 countries.
Funding
Abstract
The bifunctional protein HtrA displays chaperone and protease activities, enabling bacteria to cope with environmental stress conditions such as heat shock or extreme pH by orchestrating protein folding or degradation. Recently, we added a novel aspect to HtrA functions by identifying HtrA of the human pathogen and class I carcinogen Helicobacter pylori (Hp) as a secreted virulence factor that cleaves the cell adhesion molecule and tumor suppressor E-cadherin. In this study, we analyzed the structural integrity and activity of oligomeric HtrA from Hp under stress conditions. Examining different parameters, HtrA oligomers were investigated by casein zymography and HtrA activity was further analyzed in in vitro cleavage assays using E-cadherin as a substrate. HtrA showed temperature-dependent disintegration of oligomers. Denaturing agents targeting hydrogen bonds within HtrA destabilized HtrA oligomers while reducing agents disrupting disulfide bonds had no effect. Optimal proteolytic activity was dependent on a neutral pH; however, addition of mono- and divalent salts or reducing agents did not interfere with proteolytic activity. These data indicate the HtrA is active under stress conditions which might support Hp colonizing in the gastric environment.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.