ArticleApplied and environmental microbiology2005
The HtrA protease of Campylobacter jejuni is required for heat and oxygen tolerance and for optimal interaction with human epithelial cells.
Article in Applied and environmental microbiology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
55 citing papers in PubMed, 98 citations in OpenAlex.
- Lactococcus cremoris decreases virulence‑associated properties, and modifies the protein profile of foodborne pathogen Campylobacter jejuni in biofilm.Gut pathogens · 2026Article
- Unraveling aerotolerancy of campylobacter jejuni and campylobacter coli using a transcriptomic approach.Scientific reports · 2026Article
- The Extracytoplasmic Protein Quality Control System in Pathogenic Campylobacterota: Its Role in Bacterial Virulence and Maintaining Cellular Envelope Proteostasis.International journal of molecular sciences · 2025Review
- Transcriptome analysis of aerotolerant and aerosensitiveFrontiers in microbiology · 2025Article
- Intricate Structure-Function Relationships: The Case of the HtrA Family Proteins from Gram-Negative Bacteria.International journal of molecular sciences · 2024Review
- Pathogenicity and virulence ofVirulence · 2024Review
- Aerotolerancy ofPathogens (Basel, Switzerland) · 2024Review
- Activation of the l-fucose utilization cluster inHeliyon · 2024Article
- Article
- Trimer stability of Helicobacter pylori HtrA is regulated by a natural mutation in the protease domain.Medical microbiology and immunology · 2023Article
- Evolution and Role of Proteases inBiomolecules · 2023Review
- Roles of Aerotolerance, Biofilm Formation, and Viable but Non-Culturable State in the Survival ofMicroorganisms · 2022Review
- Campylobacter Virulence Factors and Molecular Host-Pathogen Interactions.Current topics in microbiology and immunology · 2021Review
- Peptidase PepP is a novel virulence factor ofGut microbes · 2020Article
- Extracellular Pneumococcal Serine Proteases Affect Nasopharyngeal Colonization.Frontiers in cellular and infection microbiology · 2020Article
- RevisitingFrontiers in cellular and infection microbiology · 2020Review
- Article
- The Anti-Microorganisms · 2019Article
- Assessing the Contribution of an HtrA Family Serine Protease DuringFrontiers in cellular and infection microbiology · 2019Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Campylobacter jejuni is a predominant cause of food-borne bacterial gastroenteritis in the developed world. We have investigated the importance of a homologue of the periplasmic HtrA protease in C. jejuni stress tolerance. A C. jejuni htrA mutant was constructed and compared to the parental strain, and we found that growth of the mutant was severely impaired both at 44 degrees C and in the presence of the tRNA analogue puromycin. Under both conditions, the level of misfolded protein is known to increase, and we propose that the heat-sensitive phenotype of the htrA mutant is caused by an accumulation of misfolded protein in the periplasm. Interestingly, we observed that the level of the molecular chaperones DnaK and ClpB was increased in the htrA mutant, suggesting that accumulation of non-native proteins in the periplasm induces the expression of cytoplasmic chaperones. While lack of HtrA reduces the oxygen tolerance of C. jejuni, the htrA mutant was not sensitive to compounds that increase the formation of oxygen radicals, such as paraquat, cumene hydroperoxide, and H2O2. Using tissue cultures of human epithelial cells (INT407), we found that the htrA mutant adhered to and invaded human epithelial cells with a decreased frequency compared to the wild-type strain. This defect may be a consequence of the observed altered morphology of the htrA mutant. Thus, our results suggest that in C. jejuni, HtrA is important for growth during stressful conditions and has an impact on virulence.
Indexed as
Identifiers
What OpenQuestion holds
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.