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Butyrate kinase (Buk) links branched-chain fatty acid biosynthesis, cold adaptation, and pathogenesis in Listeria monocytogenes

ABSTRACT: The phosphate acetyltransferase Ptb and butyrate kinase Buk constitute a proposed alternative route for short-chain acyl-CoA and branched-chain fatty acid (BCFA) precursor metabolism in Listeria monocytogenes. We constructed in-frame deletion mutants of ptb and buk in L. monocytogenes F2365 and found that Buk, but not Ptb, is required for anteiso-BCFA biosynthesis and cold tolerance. The buk mutant displayed reduced anteiso-BCFAs and a shift in phosphatidylglycerol (PG) composition, indicating substantial membrane remodeling. Functionally, the buk mutant exhibited defects in cell-to-cell spread, intracellular replication, phospholipase activity, LLO production, and in vivo virulence, whereas ptb retained wild-type phenotypes. Transcriptomic profiling revealed coordinated metabolic reprogramming in the buk mutant, characterized by downregulation of branched-chain amino acid (BCAA) biosynthesis and phosphotransferase (PTS) systems, indicating impaired precursor supply and nutrient acquisition, along with compensatory upregulation of central metabolism and redox processes. These findings identify Buk for the first time as a metabolic and virulence determinant in L. monocytogenes.

ORGANISM(S): Listeria monocytogenes

PROVIDER: GSE334468 | GEO | 2026/06/05

REPOSITORIES: GEO

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Project description:Listeria monocytogenes causes listeriosis, an infectious and potentially fatal disease of animals and humans. A diverse network of transcriptional regulators, including LysR-type catabolite control protein C (CcpC), is critical for the survival of L. monocytogenes and its ability to transition into the host environment. In this study, we explored the physiological and genetic consequences of deleting ccpC and the effects of such deletion on the ability of L. monocytogenes to cause disease. We found that ccpC deletion did not impact hemolytic activity, whereas it resulted in significant reductions in phospholipase activities. Western blotting revealed that the ΔccpC strain produced significantly reduced levels of the cholesterol-dependent cytolysin LLO relative to the wildtype F2365 strain. However, the ΔccpC mutant displayed no significant intracellular growth defect in macrophages. Furthermore, ΔccpC strain exhibited reduction in plaque numbers in fibroblasts compared to F2365, but plaque size was not significantly affected by ccpC deletion. In a murine model system, the ΔccpC strain exhibited a significantly reduced bacterial burden in the liver and spleen compared to the wildtype F2365 strain. Interestingly, the deletion of this gene also enhanced the survival of L. monocytogenes under conditions of H2O2-induced oxidative stress. Transcriptomic analyses performed under H2O2-induced oxidative stress conditions revealed that DNA repair, cellular responses to DNA damage and stress, metalloregulatory proteins, and genes involved in the biosynthesis of peptidoglycan and teichoic acids were significantly induced in the ccpC deletion strain relative to F2365. In contrast, genes encoding internalin, 1-phosphatidylinositol phosphodiesterase, and genes associated with sugar-specific phosphotransferase system components, porphyrin, branched-chain amino acids, and pentose phosphate pathway were significantly downregulated in the ccpC deletion strain relative to F2365. This finding highlights CcpC as a key factor that regulates L. monocytogenes physiology and responses to oxidative stress by controlling the expression of important metabolic pathways.

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Butyrate kinase (Buk) links branched-chain fatty acid biosynthesis, cold adaptation, and pathogenesis in Listeria monocytogenes

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