ArticleThe Journal of biological chemistry2009
New insights into the early steps of phosphatidylinositol mannoside biosynthesis in mycobacteria: PimB' is an essential enzyme of Mycobacterium smegmatis.
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
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Who cites it
45 citing papers in PubMed, 81 citations in OpenAlex.
- Essential role of MptB in the biosynthesis of phosphatidylinositol mannosides, lipomannan and lipoarabinomannan in mycobacteria.The Journal of biological chemistry · 2026Article
- Deficiency of the Mycobacterial Lipoarabinomannan Biosynthesis Glycosyltransferase MptC Enhances Antibacterial Immune Response and Rifapicin Antibiotic Susceptibility.Antibiotics (Basel, Switzerland) · 2026Article
- Contribution of Proteins to Membrane and Cell Wall Structures in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Functional and mechanistic characterization of the phosphatidyl-Frontiers in cellular and infection microbiology · 2026Article
- Article
- Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimE.Nature communications · 2025Article
- Detergent-induced quantitatively limited formation of diacyl phosphatidylinositol dimannoside in Mycobacterium smegmatis.Journal of lipid research · 2024Article
- Lipoarabinomannan mediates localized cell wall integrity during division in mycobacteria.Nature communications · 2024Article
- Acylation of glycerolipids in mycobacteria.Nature communications · 2023Article
- Azido Inositol Probes Enable Metabolic Labeling of Inositol-Containing Glycans and Reveal an Inositol Importer in Mycobacteria.ACS chemical biology · 2023Article
- Intrabacterial Regulation of a Cytotoxic Effector by Its Cognate Metaeffector Promotes Legionella pneumophila Virulence.mSphere · 2023Article
- Dilute Bicelles for Glycosyltransferase Studies, Novel Bicelles with Phosphatidylinositol.The journal of physical chemistry. B · 2022Article
- Crystal structure of the putative cell-wall lipoglycan biosynthesis protein LmcA from Mycobacterium smegmatis.Acta crystallographica. Section D, Structural biology · 2022Article
- Structural basis for SdgB- and SdgA-mediated glycosylation of staphylococcal adhesive proteins.Acta crystallographica. Section D, Structural biology · 2021Article
- Fluorescence Imaging-Based Discovery of Membrane Domain-Associated Proteins inJournal of bacteriology · 2021Article
- Molecular ruler mechanism and interfacial catalysis of the integral membrane acyltransferase PatA.Science advances · 2021Article
- A Glycolipid Glycosyltransferase with Broad Substrate Specificity from the Marine Bacterium "Applied and environmental microbiology · 2021Article
- The Phosphatidyl-Journal of bacteriology · 2021Article
- Antibiotics and resistance: the two-sided coin of the mycobacterial cell wall.Cell surface (Amsterdam, Netherlands) · 2020Review
- Polysaccharide Succinylation Enhances the Intracellular Survival ofACS infectious diseases · 2020Article
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Phosphatidyl-myo-inositol mannosides (PIMs) are key glycolipids of the mycobacterial cell envelope. They are considered not only essential structural components of the cell but also important molecules implicated in host-pathogen interactions. Although their chemical structures are well established, knowledge of the enzymes and sequential events leading to their biosynthesis is still incomplete. Here we show for the first time that although both mannosyltransferases PimA and PimB' (MSMEG_4253) recognize phosphatidyl-myo-inositol (PI) as a lipid acceptor, PimA specifically catalyzes the transfer of a Manp residue to the 2-position of the myo-inositol ring of PI, whereas PimB' exclusively transfers to the 6-position. Moreover, whereas PimB' can catalyze the transfer of a Manp residue onto the PI-monomannoside (PIM1) product of PimA, PimA is unable in vitro to transfer Manp onto the PIM1 product of PimB'. Further assays using membranes from Mycobacterium smegmatis and purified PimA and PimB' indicated that the acylation of the Manp residue transferred by PimA preferentially occurs after the second Manp residue has been added by PimB'. Importantly, genetic evidence is provided that pimB' is an essential gene of M. smegmatis. Altogether, our results support a model wherein Ac1PIM2, a major form of PIMs produced by mycobacteria, arises from the consecutive action of PimA, followed by PimB', and finally the acyltransferase MSMEG_2934. The essentiality of these three enzymes emphasizes the interest of novel anti-tuberculosis drugs targeting the initial steps of PIM biosynthesis.
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