ArticleInfection and immunity2001
Mycobacterium tuberculosis chaperonin 60.1 is a more potent cytokine stimulator than chaperonin 60.2 (Hsp 65) and contains a CD14-binding domain.
Article in Infection and immunity, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
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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.
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Who cites it
55 citing papers in PubMed, 123 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- Functional impact of a conservative missense mutation in the Mycobacterium bovis BCG Moreau heat shock response regulator hrcA gene.BMC microbiology · 2026Article
- Prominent transcriptomic changes in Mycobacterium intracellulare under acidic and oxidative stress.BMC genomics · 2024Article
- Role of pattern recognition receptors in sensingHeliyon · 2023Review
- Mechanisms of aPharmaceutics · 2023Article
- Detection of a target protein (GroEl2) in Mycobacterium tuberculosis using a derivative of 1,2,4-triazolethiols.Molecular diversity · 2022Article
- Innate Immune Pattern Recognition Receptors of Mycobacterium tuberculosis: Nature and Consequences for Pathogenesis of Tuberculosis.Advances in experimental medicine and biology · 2021Article
- The Russian Doll Model: How Bacteria Shape Successful and Sustainable Inter-Kingdom Relationships.Frontiers in microbiology · 2020Review
- Characterization of membrane vesicles released by Mycobacterium avium in response to environment mimicking the macrophage phagosome.Future microbiology · 2019Article
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
- Mycobacterium tuberculosis GroEL2 Modulates Dendritic Cell Responses.Infection and immunity · 2018Article
- Article
- Molecular basis of mycobacterial survival in macrophages.Cellular and molecular life sciences : CMLS · 2017Review
- Interaction of the CD43 Sialomucin with the Mycobacterium tuberculosis Cpn60.2 Chaperonin Leads to Tumor Necrosis Factor Alpha Production.Infection and immunity · 2017Article
- CD14-159C/T polymorphism in the development of delayed skin hypersensitivity to tuberculin.PloS one · 2017Article
- Importance of the C-terminal histidine residues of Helicobacter pylori GroES for Toll-like receptor 4 binding and interleukin-8 cytokine production.Scientific reports · 2016Article
- A review on host-pathogen interactions: classification and prediction.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2016Review
- Alarmins and Antitumor Immunity.Clinical therapeutics · 2016Review
- IL12, IL10, IFNγ and TNFα Expression in Human Primary Monocytes Stimulated with Bacterial Heat Shock GroEL (Hsp64) Protein.PloS one · 2016Article
- Genomic expression catalogue of a global collection of BCG vaccine strains show evidence for highly diverged metabolic and cell-wall adaptations.Scientific reports · 2015Article
Corrections and comments
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Authors and funding
9 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Much attention has focused on the Mycobacterium tuberculosis molecular chaperone chaperonin (Cpn) 60.2 (Hsp 65) in the pathology of tuberculosis because of its immunogenicity and ability to directly activate human monocytes and vascular endothelial cells. However, M. tuberculosis is one of a small group of bacteria that contain multiple genes encoding Cpn 60 proteins. We have now cloned and expressed both M. tuberculosis proteins and report that the novel chaperonin 60, Cpn 60.1, is a more potent inducer of cytokine synthesis than is Cpn 60.2. This is in spite of 76% amino acid sequence similarity between the two mycobacterial chaperonins. The M. tuberculosis Cpn 60.2 protein activates human peripheral blood mononuclear cells by a CD14-independent mechanism, whereas Cpn 60.1 is partially CD14 dependent and contains a peptide sequence whose actions are blocked by anti-CD14 monoclonal antibodies. The cytokine-inducing activity of both chaperonins is extremely resistant to heat. Cpn 60.1 may be an important virulence factor in tuberculosis, able to activate cells by diverse receptor-driven mechanisms.
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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.