Laurent Kremer

TL;DR: This study provides the first evidence for an enzymatic release of free mycolic acids from cell envelope mycolates during mycobacterial growth, and suggests the presence of a TDM-specific esterase in M. tuberculosis.

TL;DR: These studies support the further exploration of KasA as a target for mycobacterial-drug development and confirm the essentiality of kasA, a genetic tool that combines conditional gene expression and specialized transduction.

TL;DR: The PPM synthase of Mycobacterium tuberculosis is identified and characterized, now termed Mt-Ppm1, which possesses an unusual two-domain architecture and transfers Man from GDP-Man to a structurally diverse range of lipid monophosphate acceptors.

TL;DR: Enzymatic studies revealed that, whereas phosphorylation decreases the activity of KasA in the elongation process of long chain fatty acids synthesis, this modification enhances that of KasB, suggesting an unusual mechanism of FAS-II system regulation, allowing pathogenic mycobacteria to produce full-length mycolates, which are required for adaptation and intracellular survival in macrophages.

TL;DR: It is confirmed that Mtb Pks13 is required for mycolic acid biosynthesis, validates it as a druggable target and demonstrates the therapeutic potential of simultaneously inhibiting multiple targets in the same biosynthetic pathway.