Discovery of a Specific Inhibitor of Pyomelanin Synthesis in Legionella pneumophila

J Med Chem. 2015 Nov 12;58(21):8402-12. doi: 10.1021/acs.jmedchem.5b01589. Epub 2015 Oct 23.

Abstract

Phenylalanine hydroxylase catalyzes the first step in the synthesis of pyomelanin, a pigment that aids in the acquisition of essential iron in certain bacteria. In this work, we present the development and application of a drug discovery protocol by targeting this enzyme in Legionella pneumophila, the major causative agent of Legionnaires' disease. We employ a combination of high-throughput screening to identify small-molecule binders, enzymatic activity measurements to identify inhibitors in vitro, and the verification of the inhibitory effect in vivo. The most potent inhibitor shows an IC50 value in the low micromolar range and successfully abolishes the synthesis of pyomelanin in L. pneumophila cultures at 10 μM. Thus, this compound represents a novel and effective tool for investigating the role of pyomelanin in the biology and pathogenicity of this organism. Altogether, the results demonstrate a successful pathway for drug development focusing on binding specificity in the initial high-throughput screening steps.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Drug Discovery
  • Enzyme Inhibitors / chemistry*
  • Enzyme Inhibitors / pharmacology*
  • Humans
  • Iron / metabolism
  • Legionella pneumophila / drug effects*
  • Legionella pneumophila / enzymology*
  • Legionella pneumophila / metabolism
  • Legionnaires' Disease / drug therapy
  • Legionnaires' Disease / microbiology*
  • Ligands
  • Melanins / antagonists & inhibitors
  • Melanins / metabolism*
  • Phenylalanine Hydroxylase / antagonists & inhibitors*
  • Phenylalanine Hydroxylase / metabolism

Substances

  • Enzyme Inhibitors
  • Ligands
  • Melanins
  • pyomelanin
  • Iron
  • Phenylalanine Hydroxylase