ArticlePloS one2014
Mycobacterium tuberculosis proteins involved in mycolic acid synthesis and transport localize dynamically to the old growing pole and septum.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.
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51 citing papers in PubMed, 84 citations in OpenAlex.
- The polar landscape of bacterial pathogens and predators.Current opinion in microbiology · 2026Review
- Structure, assembly, and mechanism of the MmpL family of transporters.Microbiology and molecular biology reviews : MMBR · 2026Review
- Polar growth factor PgfA regulates polar peptidoglycan synthesis as well as mycolate synthesis inJournal of bacteriology · 2026Article
- Linking lipid profile alterations to antibiotic tolerance and natural product synergy in drug-resistant Mycobacterium tuberculosis clinical isolates.Scientific reports · 2026Article
- A split ALFA tag-nanobody system for protein localization and proximity proteomics in mycobacteria.mBio · 2025Article
- Article
- Structural modeling and characterization of the Mycobacterium tuberculosis MmpL3 C-terminal domain.FEBS letters · 2024Article
- MmpL3, Wag31, and PlrA are involved in coordinating polar growth with peptidoglycan metabolism and nutrient availability.Journal of bacteriology · 2024Article
- MmpL3, Wag31 and PlrA are involved in coordinating polar growth with peptidoglycan metabolism and nutrient availability.bioRxiv : the preprint server for biology · 2024Article
- Mycobacterial Targets for Thiourea Derivatives: Opportunities for Virtual Screening in Tuberculosis Drug Discovery.Current medicinal chemistry · 2024Review
- Spatial segregation and aging of metabolic processes underlie phenotypic heterogeneity in mycobacteria.bioRxiv : the preprint server for biology · 2023Article
- Recent advances in mycobacterial membrane protein large 3 inhibitor drug design for mycobacterial infections.Expert opinion on drug discovery · 2023Review
- Molecular Mechanisms of MmpL3 Function and Inhibition.Microbial drug resistance (Larchmont, N.Y.) · 2023Review
- In vivo imaging of MmpL transporters reveals distinct subcellular locations for export of mycolic acids and non-essential trehalose polyphleates in the mycobacterial outer membrane.Scientific reports · 2023Article
- Proton transfer activity of the reconstitutedProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Localization of EccABMC microbiology · 2022Article
- A Novel Acyl-AcpM-Binding Protein Confers Intrinsic Sensitivity to Fatty Acid Synthase Type II Inhibitors inFrontiers in microbiology · 2022Article
- Spatiotemporal localization of proteins in mycobacteria.Cell reports · 2021Article
- Intracellular localisation of Mycobacterium tuberculosis affects efficacy of the antibiotic pyrazinamide.Nature communications · 2021Article
- Article
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Authors and funding
8 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Understanding the mechanism that controls space-time coordination of elongation and division of Mycobacterium tuberculosis (Mtb), the causative agent of tuberculosis (TB), is critical for fighting the tubercle bacillus. Most of the numerous enzymes involved in the synthesis of Mycolic acid - Arabinogalactan-Peptidoglycan complex (MAPc) in the cell wall are essential in vivo. Using a dynamic approach, we localized Mtb enzymes belonging to the fatty acid synthase-II (FAS-II) complexes and involved in mycolic acid (MA) biosynthesis in a mycobacterial model of Mtb: M. smegmatis. Results also showed that the MA transporter MmpL3 was present in the mycobacterial envelope and was specifically and dynamically accumulated at the poles and septa during bacterial growth. This localization was due to its C-terminal domain. Moreover, the FAS-II enzymes were co-localized at the poles and septum with Wag31, the protein responsible for the polar localization of mycobacterial peptidoglycan biosynthesis. The dynamic localization of FAS-II and of the MA transporter with Wag31, at the old-growing poles and at the septum suggests that the main components of the mycomembrane may potentially be synthesized at these precise foci. This finding highlights a major difference between mycobacteria and other rod-shaped bacteria studied to date. Based on the already known polar activities of envelope biosynthesis in mycobacteria, we propose the existence of complex polar machinery devoted to the biogenesis of the entire envelope. As a result, the mycobacterial pole would represent the Achilles' heel of the bacillus at all its growing stages.
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