cAMP Receptor Protein of Salmonella enterica Serovar Typhimurium Modulate Glycolysis in Macrophages to Induce Cell Apoptosis

Curr Microbiol. 2019 Jan;76(1):1-6. doi: 10.1007/s00284-018-1574-1. Epub 2018 Oct 12.

Abstract

We studied the role of glycolysis in the mechanism of cAMP receptor protein-induced macrophage cell death of Salmonella enterica serovar Typhimurium (S. Typhimurium). Cell apoptosis, caspase-3, -8, -9 enzyme activity, and pyruvic acid, lactic acid, ATP, and hexokinase (HK) contents were determined after infection of macrophages with S. Typhimurium SL1344 wild-type and a cAMP receptor protein mutant strain. While cell apoptosis, caspase-3, -8, -9 enzyme activity, lactic acid, hexokinase, and ATP levels significantly changed by infection with crp mutants compared to the wild-type strain (P < 0.05). Our data suggest that the cAMP receptor protein of S. Typhimurium can modulate macrophage death by effecting glycolysis levels. This finding may help to elucidate the mechanisms of S. Typhimurium pathogenesis.

MeSH terms

  • Adenosine Triphosphate / analysis
  • Animals
  • Apoptosis / physiology*
  • Caspase 3 / metabolism
  • Caspase 8 / metabolism
  • Caspase 9 / metabolism
  • Cell Line
  • Cyclic AMP Receptor Protein / genetics*
  • Cyclic AMP Receptor Protein / metabolism*
  • Glycolysis / physiology*
  • Hexokinase / analysis
  • Lactic Acid / analysis
  • Macrophages / metabolism*
  • Mice
  • Pyruvic Acid / analysis
  • RAW 264.7 Cells
  • Salmonella typhimurium / genetics
  • Salmonella typhimurium / metabolism*
  • Salmonella typhimurium / pathogenicity

Substances

  • Cyclic AMP Receptor Protein
  • Lactic Acid
  • Pyruvic Acid
  • Adenosine Triphosphate
  • Hexokinase
  • Caspase 3
  • Caspase 8
  • Caspase 9