ArticleThe Journal of biological chemistry2009
A lipid profile typifies the Beijing strains of Mycobacterium tuberculosis: identification of a mutation responsible for a modification of the structures of phthiocerol dimycocerosates and phenolic glycolipids.
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 31 papers.
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31 citing papers in PubMed, 62 citations in OpenAlex.
- Rv3787c Influences Growth Dynamics ofBiology · 2026Article
- Protein-Mediated Virulence in Mycobacterium tuberculosis.Advances in experimental medicine and biology · 2026Review
- Mycobacterial Phenolic Glycolipid Triggers ATP-Mediated Neuronal P2X3 Signaling and Cough.bioRxiv : the preprint server for biology · 2025Article
- Comparative Transcriptomics Reveal Differential Expression of Coding and Non-Coding RNAs in Clinical Strains ofInternational journal of molecular sciences · 2024Article
- Drug resistant Mycobacterium tuberculosis strains have altered cell envelope hydrophobicity that influences infection outcomes in human macrophages.Scientific reports · 2024Article
- Drug resistantbioRxiv : the preprint server for biology · 2024Article
- Bioorthogonal Metabolic Labeling of the Virulence Factor Phenolic Glycolipid in Mycobacteria.ACS chemical biology · 2024Article
- Exposure ofFrontiers in tuberculosis · 2024Article
- Article
- Lack of methoxy-mycolates characterizes the geographically restricted lineage 7 ofMicrobial genomics · 2023Article
- Clinical strains of Mycobacterium tuberculosis exhibit differential lipid metabolism-associated transcriptome changes in in vitro cholesterol and infection models.Pathogens and disease · 2023Article
- Sub-Lineage Specific Phenolic Glycolipid Patterns in theFrontiers in microbiology · 2022Article
- Genetic Diversity inAnnual review of genetics · 2020Review
- Article
- Higher genome mutation rates of Beijing lineage of Mycobacterium tuberculosis during human infection.Scientific reports · 2020Article
- Host Cell Targets of Released Lipid and Secreted Protein Effectors ofFrontiers in cellular and infection microbiology · 2020Review
- Mycobacterial Evolution Intersects With Host Tolerance.Frontiers in immunology · 2019Review
- Methodological and Clinical Aspects of the Molecular Epidemiology of Mycobacterium tuberculosis and Other Mycobacteria.Clinical microbiology reviews · 2016Review
- Differential influence of nutrient-starved Mycobacterium tuberculosis on adaptive immunity results in progressive tuberculosis disease and pathology.Infection and immunity · 2015Article
- Correlates between models of virulence for Mycobacterium tuberculosis among isolates of the Central Asian lineage: a case for lysozyme resistance testing?Infection and immunity · 2015Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Mycobacterium tuberculosis Beijing strains are a family highly prevalent in Asia and have recently spread worldwide, causing a number of epidemics, suggesting that they express virulence factors not found in other M. tuberculosis strains. Accordingly, we looked for putative characteristic compounds by comparing the lipid profiles of several Beijing and non-Beijing strains. All the Beijing strains analyzed were found to synthesize structural variants of two well known characteristic lipids of the tubercle bacillus, namely phthiocerol dimycocerosates (DIM) and eventually phenolglycolipids (PGL). These variants were not found in non-Beijing M. tuberculosis isolates. Structural elucidation of these variants showed that they consist of phthiotriol and glycosylated phenolphthiotriol dimycocerosates, eventually acylated with 1 mol of palmitic acid, in addition to the conventional acylation of the beta-diol by mycocerosic acids. We demonstrated that this unusual lipid profile resulted from a single point mutation in the Rv2952 gene, which encodes the S-adenosylmethionine-dependent methyltransferase participating to the O-methylation of the third hydroxyl of the phthiotriol and phenolphthiotriol in the biosynthetic pathway of DIM and PGL. Consistently, the mutated enzyme exhibited in vitro a much lower O-methyltransferase activity than did the wild-type Rv2952. We finally demonstrated that the structural variants of DIM and PGL fulfill the same function in the cell envelope and virulence than their conventional counterparts.
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