ArticleInfection and immunity2008
A Mycobacterium tuberculosis mutant lacking the groEL homologue cpn60.1 is viable but fails to induce an inflammatory response in animal models of infection.
Article in Infection and immunity, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 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.
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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
47 citing papers in PubMed, 118 citations in OpenAlex.
- Seryl phosphorylation modulates chaperonin function of Mycobacterial chaperonin, Cpn60.1.Cell stress & chaperones · 2026Article
- The Sialomucin CD43 Drives Tuberculosis Immunopathology Across Different Host Genetic Backgrounds.Inflammation · 2026Article
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Structural and Functional Characterization of Protein Adhesins and Pili in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Article
- Analysis of the components of Mycobacterium tuberculosis heat-resistant antigen (Mtb-HAg) and its regulation of γδ T-cell function.Cellular & molecular biology letters · 2024Article
- Polypharmacology-Driven Discovery and Design of Highly Selective, Dual and Multitargeting Inhibitors ofCurrent drug targets · 2024Review
- Characterization of Molecular Chaperone GroEL as a Potential Virulence Factor inFoods (Basel, Switzerland) · 2023Article
- Mycobacterial chaperonins in cellular proteostasis: Evidence for chaperone function of Cpn60.1 and Cpn60.2-mediated protein folding.Molecular microbiology · 2023Article
- DprE2 is a molecular target of the anti-tubercular nitroimidazole compounds pretomanid and delamanid.Nature communications · 2023Article
- Mechanisms of aPharmaceutics · 2023Article
- Nitrogen metabolism in mycobacteria: the key genes and targeted antimicrobials.Frontiers in microbiology · 2023Review
- Article
- Comprehensive Molecular Dissection ofInternational journal of molecular sciences · 2021Article
- Determination of variable region sequences from hybridoma immunoglobulins that target Mycobacterium tuberculosis virulence factors.PloS one · 2021Article
- Analogs of nitrofuran antibiotics are potent GroEL/ES inhibitor pro-drugs.Bioorganic & medicinal chemistry · 2020Article
- Multitargeting Compounds: A Promising Strategy to Overcome Multi-Drug Resistant Tuberculosis.Molecules (Basel, Switzerland) · 2020Review
- Dual-targeting GroEL/ES chaperonin and protein tyrosine phosphatase B (PtpB) inhibitors: A polypharmacology strategy for treating Mycobacterium tuberculosis infections.Bioorganic & medicinal chemistry letters · 2019Article
- HSP60/10 chaperonin systems are inhibited by a variety of approved drugs, natural products, and known bioactive molecules.Bioorganic & medicinal chemistry letters · 2019Article
- Targeting the Proteostasis Network for Mycobacterial Drug Discovery.ACS infectious diseases · 2018Review
- A Glimpse Into the Structure and Function of Atypical Type I Chaperonins.Frontiers in molecular biosciences · 2018Review
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
Abstract
The causative agent of tuberculosis, Mycobacterium tuberculosis, has two chaperonin (Cpn60) proteins and one cochaperonin (Cpn10) protein. We show here that cpn60.2 and cpn10, but not cpn60.1, are essential for cell survival. A mutant lacking Cpn60.1 was indistinguishable from the wild-type organism in plate and broth culture and within murine macrophages, although it showed increased sensitivity to high temperature (55 degrees C). However, infection of mice with the Deltacpn60.1 mutant revealed a major difference from the wild-type organism. In spite of having equal numbers of bacteria in infected sites, the Deltacpn60.1 mutant failed to produce granulomatous inflammation in either mice or guinea pigs. This was associated with reduced cytokine expression in infected animals and macrophages. Cell wall lipid acid composition was not altered in the mutant strain. Thus, it appears that Cpn60.1 is an important agent in the regulation of the cytokine-dependent granulomatous response in M. tuberculosis infection.
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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.