ArticleBMC microbiology2013
Lipoproteins of slow-growing Mycobacteria carry three fatty acids and are N-acylated by apolipoprotein N-acyltransferase BCG_2070c.
Article in BMC microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 31 citations in OpenAlex.
- Sec and Tat Mediated Secretion Safeguards Mycobacterium tuberculosis Membrane Homeostasis.Molecular & cellular proteomics : MCP · 2026Article
- Metabolic Tagging Reveals Surface-Associated Lipoproteins in Mycobacteria.ACS infectious diseases · 2025Article
- Metabolic tagging reveals surface-associated lipoproteins in mycobacteria.bioRxiv : the preprint server for biology · 2025Article
- Decoding drug tolerance: insights into theFrontiers in microbiology · 2025Article
- Genetic and chemical control of tuberculostearic acid production inMicrobiology spectrum · 2024Article
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- Label-Free Comparative Proteomics of Differentially ExpressedPathogens (Basel, Switzerland) · 2021Article
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- Hydrophobic Mycobacterial Antigens Elicit Polyfunctional T Cells inFrontiers in immunology · 2020Article
- Article
- Molecular Mechanisms of Intrinsic Streptomycin Resistance in Mycobacterium abscessus.Antimicrobial agents and chemotherapy · 2018Article
- Lipid moieties on lipoproteins of commensal and non-commensal staphylococci induce differential immune responses.Nature communications · 2017Article
- Structural insights into lipoprotein N-acylation byProceedings of the National Academy of Sciences of the United States of America · 2017Article
- Identification of the Lyso-FormJournal of bacteriology · 2017Article
- Scrutiny of Mycobacterium tuberculosis 19 kDa antigen proteoforms provides new insights in the lipoglycoprotein biogenesis paradigm.Scientific reports · 2017Article
- Lipoprotein Glycosylation by Protein-Frontiers in microbiology · 2017Article
- Toward Understanding the Essence of Post-Translational Modifications for the Mycobacterium tuberculosis Immunoproteome.Frontiers in immunology · 2014Review
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3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundLipoproteins are virulence factors of Mycobacterium tuberculosis. Bacterial lipoproteins are modified by the consecutive action of preprolipoprotein diacylglyceryl transferase (Lgt), prolipoprotein signal peptidase (LspA) and apolipoprotein N- acyltransferase (Lnt) leading to the formation of mature triacylated lipoproteins. Lnt homologues are found in Gram-negative and high GC-rich Gram-positive, but not in low GC-rich Gram-positive bacteria, although N-acylation is observed. In fast-growing Mycobacterium smegmatis, the molecular structure of the lipid modification of lipoproteins was resolved recently as a diacylglyceryl residue carrying ester-bound palmitic acid and ester-bound tuberculostearic acid and an additional amide-bound palmitic acid.
resultsWe exploit the vaccine strain Mycobacterium bovis BCG as model organism to investigate lipoprotein modifications in slow-growing mycobacteria. Using Escherichia coli Lnt as a query in BLASTp search, we identified BCG_2070c and BCG_2279c as putative lnt genes in M. bovis BCG. Lipoproteins LprF, LpqH, LpqL and LppX were expressed in M. bovis BCG and BCG_2070c lnt knock-out mutant and lipid modifications were analyzed at molecular level by matrix-assisted laser desorption ionization time-of-flight/time-of-flight analysis. Lipoprotein N-acylation was observed in wildtype but not in BCG_2070c mutants. Lipoprotein N- acylation with palmitoyl and tuberculostearyl residues was observed.
conclusionsLipoproteins are triacylated in slow-growing mycobacteria. BCG_2070c encodes a functional Lnt in M. bovis BCG. We identified mycobacteria-specific tuberculostearic acid as further substrate for N-acylation in slow-growing mycobacteria.
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