ArticlePLoS pathogens2020
Protein kinases PknA and PknB independently and coordinately regulate essential Mycobacterium tuberculosis physiologies and antimicrobial susceptibility.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 60 citations in OpenAlex.
- The structural context of mutations in proteins predicts their effect on antibiotic resistance.eLife · 2026Article
- Structural insights into multitargetingMicrobiology spectrum · 2026Article
- Structural Modification of Indole Derivatives as PknB Inhibitors for Enhanced Enzymatic Inhibition and Antimycobacterial Activity.ACS omega · 2026Article
- Polypharmacology is an enduring and nearly universal property of kinase inhibitors.bioRxiv : the preprint server for biology · 2026Article
- Multiple input-multiple output (MIMO) designs in two-component signalling systems of Mycobacterium tuberculosis.FEMS microbiology reviews · 2026Review
- The role of colony morphotype in shaping gene essentiality inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- PknB and STP as potential targets of luteolin in combating Trueperella pyogenes infections.Scientific reports · 2025Article
- In Vitro Activity of the Triazinyl Diazepine Compound FTSD2 Against Drug-ResistantPharmaceuticals (Basel, Switzerland) · 2025Article
- Repurposing of apoptotic inducer drugs against Mycobacterium tuberculosis.Scientific reports · 2025Article
- Structural modeling and characterization of the Mycobacterium tuberculosis MmpL3 C-terminal domain.FEBS letters · 2024Article
- Phosphorylation of VapB antitoxins affects intermolecular interactions to regulate VapC toxin activity inJournal of bacteriology · 2024Article
- Experimental measurement and computational prediction of bacterial Hanks-type Ser/Thr signaling system regulatory targets.Molecular microbiology · 2024Review
- Identification and Design of Novel Potential Antimicrobial Peptides Targeting Mycobacterial Protein Kinase PknB.The protein journal · 2024Article
- Phosphorylation of VapB antitoxins affects intermolecular interactions to regulate VapC toxin activity inbioRxiv : the preprint server for biology · 2024Article
- Review
- Regulatory Intersection of Two-component System and Ser/Thr Protein Kinase Signaling in Mycobacterium tuberculosis.Journal of molecular biology · 2024Article
- Spatial segregation and aging of metabolic processes underlie phenotypic heterogeneity in mycobacteria.bioRxiv : the preprint server for biology · 2023Article
- Discovery of novel reversible inhibitor of DprE1 based on benzomorpholine for the treatment of tuberculosis.Microbiology spectrum · 2023Article
- Molecular Mechanisms of MmpL3 Function and Inhibition.Microbial drug resistance (Larchmont, N.Y.) · 2023Review
- The Mycobacterium tuberculosis protein O-phosphorylation landscape.Nature microbiology · 2023Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 1 country.
Funding
Abstract
The Mycobacterium tuberculosis Ser/Thr protein kinases PknA and PknB are essential for growth and have been proposed as possible drug targets. We used a titratable conditional depletion system to investigate the functions of these kinases. Depletion of PknA or PknB or both kinases resulted in growth arrest, shortening of cells, and time-dependent loss of acid-fast staining with a concomitant decrease in mycolate synthesis and accumulation of trehalose monomycolate. Depletion of PknA and/or PknB resulted in markedly increased susceptibility to β-lactam antibiotics, and to the key tuberculosis drug rifampin. Phosphoproteomic analysis showed extensive changes in protein phosphorylation in response to PknA depletion and comparatively fewer changes with PknB depletion. These results identify candidate substrates of each kinase and suggest specific and coordinate roles for PknA and PknB in regulating multiple essential physiologies. These findings support these kinases as targets for new antituberculosis drugs and provide a valuable resource for targeted investigation of mechanisms by which protein phosphorylation regulates pathways required for growth and virulence in M. tuberculosis.
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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.