ArticleJournal of bacteriology2009
Survival of pathogenic mycobacteria in macrophages is mediated through autophosphorylation of protein kinase G.
Article in Journal of bacteriology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 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
26 citing papers in PubMed, 60 citations in OpenAlex.
- Physiological, genetical and morphological alterations in Mycobacterium avium subsp. paratuberculosis mutants generated with the CRISPRi system.BMC microbiology · 2026Article
- A Phosphoproteomic Analysis of Mycobacterial PknG-Mediated Host Immune Evasion.Journal of proteome research · 2025Article
- Protein kinase G-a key regulator of pathogenesis in Mycobacterium tuberculosis infection.Archives of microbiology · 2025Review
- S-nitrosylation-triggered secretion of mycobacterial PknG leads to phosphorylation of SODD to prevent apoptosis of infected macrophages.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Article
- "It Takes Two to Tango": Role of Neglected Macrophage Manipulators Coronin 1 and Protein Kinase G in Mycobacterial Pathogenesis.Frontiers in cellular and infection microbiology · 2020Review
- Predictive Binding Affinity of Plant-Derived Natural Products Towards the Protein Kinase G Enzyme ofPlants (Basel, Switzerland) · 2019Article
- Tyrosine Phosphorylation as a Widespread Regulatory Mechanism in Prokaryotes.Journal of bacteriology · 2019Review
- Identification of Novel Physiological Substrates ofMolecular & cellular proteomics : MCP · 2018Article
- PknG supports mycobacterial adaptation in acidic environment.Molecular and cellular biochemistry · 2018Article
- Article
- Epigenetic Phosphorylation Control of Mycobacterium tuberculosis Infection and Persistence.Microbiology spectrum · 2017Review
- Oxidative Unfolding of the Rubredoxin Domain and the Natively Disordered N-terminal Region Regulate the Catalytic Activity of Mycobacterium tuberculosis Protein Kinase G.The Journal of biological chemistry · 2016Article
- Protein kinase A (PknA) of Mycobacterium tuberculosis is independently activated and is critical for growth in vitro and survival of the pathogen in the host.The Journal of biological chemistry · 2015Article
- Nontuberculous mycobacterial osteomyelitis.Infectious diseases (London, England) · 2015Review
- Crosstalk between Mycobacterium tuberculosis and the host cell.Seminars in immunology · 2014Review
- Identification of Ser/Thr kinase and forkhead associated domains in Mycobacterium ulcerans: characterization of novel association between protein kinase Q and MupFHA.PLoS neglected tropical diseases · 2014Article
- Bacterial serine/threonine protein kinases in host-pathogen interactions.The Journal of biological chemistry · 2014Review
- Inflammatory stimuli reprogram macrophage phagocytosis to macropinocytosis for the rapid elimination of pathogens.PLoS pathogens · 2014Article
- 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
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Pathogenic mycobacteria survive within macrophages through the inhibition of phagosome-lysosome fusion. A crucial factor for avoiding lysosomal degradation is the mycobacterial serine/threonine protein kinase G (PknG). PknG is released into the macrophage cytosol upon mycobacterial infection, suggesting that PknG might exert its activity by interfering with host signaling cascades, but the mode of action of PknG remains unknown. Here, we show that PknG undergoes autophosphorylation on threonine residues located at the N terminus. In contrast to all other mycobacterial kinases investigated thus far, autophosphorylation of PknG was not involved in the regulation of its kinase activity. However, autophosphorylation was crucial for the capacity of PknG to promote mycobacterial survival within macrophages. These results will contribute to a better understanding of the virulence mechanisms of pathogenic mycobacteria and may help to design improved inhibitors of PknG to be developed as antimycobacterial compounds.
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.