ArticleApplied and environmental microbiology2011
Different contributions of HtrA protease and chaperone activities to Campylobacter jejuni stress tolerance and physiology.
Article in Applied and environmental microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 56 citations in OpenAlex.
- Serine protease HtrA promotesScience advances · 2026Article
- Lactococcus cremoris decreases virulence‑associated properties, and modifies the protein profile of foodborne pathogen Campylobacter jejuni in biofilm.Gut pathogens · 2026Article
- Heterologous Expression, Purification, and Characterization of a High-Temperature Requirement A (HtrA) Protease Homologue from Leptospira.Applied biochemistry and biotechnology · 2025Article
- 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
- ClpB enhances thermotolerance inMicrobiology spectrum · 2025Article
- Antibiotic-induced stress responses in Gram-negative bacteria and their role in antibiotic resistance.The Journal of antimicrobial chemotherapy · 2025Review
- 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
- Article
- Evolution and Role of Proteases inBiomolecules · 2023Review
- Identification of genes associated with environmental persistence in Campylobacter jejuni and Campylobacter coli isolates from processing in a broiler abattoir.Veterinary research communications · 2022Article
- Campylobacter Virulence Factors and Molecular Host-Pathogen Interactions.Current topics in microbiology and immunology · 2021Review
- Shedding light on the bacterial resistance to toxic UV filters: a comparative genomic study.PeerJ · 2021Article
- Functional analysis and cryo-electron microscopy ofGut microbes · 2020Article
- Whole genome sequencing reveals extended natural transformation in Campylobacter impacting diagnostics and the pathogens adaptive potential.Scientific reports · 2020Article
- Differences in the Transcriptomic Response ofFrontiers in microbiology · 2020Article
- Chaperone activity of serine protease HtrA of Helicobacter pylori as a crucial survival factor under stress conditions.Cell communication and signaling : CCS · 2019Article
- Establishment of serine protease htrA mutants in Helicobacter pylori is associated with secA mutations.Scientific reports · 2019Article
- Quantification of serine protease HtrA molecules secreted by the foodborne pathogenGut pathogens · 2019Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The microaerophilic bacterium Campylobacter jejuni is the most common cause of bacterial food-borne infections in the developed world. Tolerance to environmental stress relies on proteases and chaperones in the cell envelope, such as HtrA and SurA. HtrA displays both chaperone and protease activities, but little is known about how each of these activities contributes to stress tolerance in bacteria. In vitro experiments showed temperature-dependent protease and chaperone activities of C. jejuni HtrA. A C. jejuni mutant lacking only the protease activity of HtrA was used to show that the HtrA chaperone activity is sufficient for growth at high temperature or under oxidative stress, whereas the HtrA protease activity is essential only under conditions close to the growth limit for C. jejuni. However, the protease activity was required to prevent induction of the cytoplasmic heat shock response even under optimal growth conditions. Interestingly, the requirement of HtrA at high temperatures was found to depend on the oxygen level, and our data suggest that HtrA may protect oxidatively damaged proteins. Finally, protease activity stimulates HtrA production and oligomer formation, suggesting that a regulatory role depends on the protease activity of HtrA. Studying a microaerophilic organism encoding only two known periplasmic chaperones (HtrA and SurA) revealed an efficient HtrA chaperone activity and proposed multiple roles of the protease activity, increasing our understanding of HtrA in bacterial physiology.
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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.