The β-lactam ticarcillin is a Staphylococcus aureus UDP-N-acetylglucosamine 2-epimerase binder

Biochimie. 2022 Jun:197:1-8. doi: 10.1016/j.biochi.2022.01.016. Epub 2022 Jan 28.

Abstract

Infectious diseases account for 25% of the causes of death worldwide and this rate is expected to increase due to antibiotic resistance. Among the bacteria associated with healthcare infections, Staphylococcus aureus is a prevalent pathogen and about 50% of the isolates are found to be methicillin-resistant. Here we describe the identification of ticarcillin as a weak binder of the S. aureus UDP-N-acetylglucosamine 2-epimerase. After a docking screening, ticarcillin was identified as a ligand in using the recently proposed isothermal analysis of differential scanning fluorimetry data. Finally, an equilibrium MD simulation confirmed the docking binding mode as a stable pose, with large contributions to the binding energy coming from interactions between Arg206 and Arg207 and the carboxylate groups in ticarcillin.

Keywords: Ligand screening; MnaA; Staphylococcus aureus; Ticarcillin; UDP-N-Acetylglucosamine 2-epimerase.

MeSH terms

  • Anti-Bacterial Agents / pharmacology
  • Carbohydrate Epimerases / metabolism
  • Methicillin-Resistant Staphylococcus aureus*
  • Staphylococcus aureus* / metabolism
  • Ticarcillin
  • beta-Lactams

Substances

  • Anti-Bacterial Agents
  • beta-Lactams
  • Carbohydrate Epimerases
  • UDP acetylglucosamine-2-epimerase
  • Ticarcillin