ArticleJournal of bacteriology2013
Regulation of host hemoglobin binding by the Staphylococcus aureus Clp proteolytic system.
Article in Journal of bacteriology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 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
34 citing papers in PubMed, 64 citations in OpenAlex.
- Unraveling proteomic chaos by independent component analysis-ClpX proficiency promotes the iron and oxygen limitation responses ofmSystems · 2025Article
- The Effect ofInternational journal of molecular sciences · 2025Article
- Mutations in the clpS Gene of Riemerella anatipestifer Affect Stress Response and Bacterial Virulence.Current microbiology · 2025Article
- Disruption of the ATP-dependent unfoldase ClpX reverses antifungal resistance in Cryptococcus neoformans.Nature communications · 2025Article
- Revealing fitness and virulence determinants of hypervirulentFrontiers in cellular and infection microbiology · 2025Article
- Coordinated adaptation ofmBio · 2024Article
- Review
- Translation Fidelity and Respiration Deficits in CLPP-Deficient Tissues: Mechanistic Insights from Mitochondrial Complexome Profiling.International journal of molecular sciences · 2023Article
- ClpP protease modulates bacterial growth, stress response, and bacterial virulence in Brucella abortus.Veterinary research · 2023Article
- A Clinically Selected Staphylococcus aureusAntimicrobial agents and chemotherapy · 2023Article
- ESKAPE Pathogens: Looking at Clp ATPases as Potential Drug Targets.Antibiotics (Basel, Switzerland) · 2022Review
- Systematic identification of molecular mediators of interspecies sensing in a community of two frequently coinfecting bacterial pathogens.PLoS biology · 2022Article
- Genome-Wide Identification of Ralstonia solanacearum Genes Required for Survival in Tomato Plants.mSystems · 2021Article
- Article
- The ClpXP Protease Contributes to Staphylococcus aureus Pneumonia.The Journal of infectious diseases · 2020Article
- Proteomics identifies a convergent innate response to infective endocarditis and extensive proteolysis in vegetation components.JCI insight · 2020Article
- Functional Characterisation of ClpP Mutations Conferring Resistance to Acyldepsipeptide Antibiotics in Firmicutes.Chembiochem : a European journal of chemical biology · 2020Article
- The Staphylococcus aureus IsdH Receptor Forms a Dynamic Complex with Human Hemoglobin that Triggers Heme Release via Two Distinct Hot Spots.Journal of molecular biology · 2020Article
- Bacterial ClpP Protease Is a Potential Target for Methyl Gallate.Frontiers in microbiology · 2020Article
- ClpP Protease, a Promising Antimicrobial Target.International journal of molecular sciences · 2019Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Protein turnover is a key process for bacterial survival mediated by intracellular proteases. Proteolytic degradation reduces the levels of unfolded and misfolded peptides that accumulate in the cell during stress conditions. Three intracellular proteases, ClpP, HslV, and FtsH, have been identified in the Gram-positive bacterium Staphylococcus aureus, a pathogen responsible for significant morbidity and mortality worldwide. Consistent with their crucial role in protein turnover, ClpP, HslV, and FtsH affect a number of cellular processes, including metabolism, stress responses, and virulence. The ClpP protease is believed to be the principal degradation machinery in S. aureus. This study sought to identify the effect of the Clp protease on the iron-regulated surface determinant (Isd) system, which extracts heme-iron from host hemoglobin during infection and is critical to S. aureus pathogenesis. Inactivation of components of the Clp protease alters abundance of several Isd proteins, including the hemoglobin receptor IsdB. Furthermore, the observed changes in IsdB abundance are the result of transcriptional regulation, since transcription of isdB is decreased by clpP or clpX inactivation. In contrast, inactivation of clpC enhances isdB transcription and protein abundance. Loss of clpP or clpX impairs host hemoglobin binding and utilization and results in severe virulence defects in a systemic mouse model of infection. These findings suggest that the Clp proteolytic system is important for regulating nutrient iron acquisition in S. aureus. The Clp protease and Isd complex are widely conserved in bacteria; therefore, these data reveal a novel Clp-dependent regulation pathway that may be present in other bacterial pathogens.
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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.