In vitro selection of Phytomonas serpens cells resistant to the calpain inhibitor MDL28170: alterations in fitness and expression of the major peptidases and efflux pumps

Parasitology. 2018 Mar;145(3):355-370. doi: 10.1017/S0031182017001561. Epub 2017 Oct 17.

Abstract

The species Phytomonas serpens is known to express some molecules displaying similarity to those described in trypanosomatids pathogenic to humans, such as peptidases from Trypanosoma cruzi (cruzipain) and Leishmania spp. (gp63). In this work, a population of P. serpens resistant to the calpain inhibitor MDL28170 at 70 µ m (MDLR population) was selected by culturing promastigotes in increasing concentrations of the drug. The only relevant ultrastructural difference between wild-type (WT) and MDLR promastigotes was the presence of microvesicles within the flagellar pocket of the latter. MDLR population also showed an increased reactivity to anti-cruzipain antibody as well as a higher papain-like proteolytic activity, while the expression of calpain-like molecules cross-reactive to anti-Dm-calpain (from Drosophila melanogaster) antibody and calcium-dependent cysteine peptidase activity were decreased. Gp63-like molecules also presented a diminished expression in MDLR population, which is probably correlated to the reduction in the parasite adhesion to the salivary glands of the insect vector Oncopeltus fasciatus. A lower accumulation of Rhodamine 123 was detected in MDLR cells when compared with the WT population, a phenotype that was reversed when MDLR cells were treated with cyclosporin A and verapamil. Collectively, our results may help in the understanding of the roles of calpain inhibitors in trypanosomatids.

Keywords: Phytomonas; calpain inhibitors; calpain-like proteins; peptidases; resistance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Calpain / antagonists & inhibitors
  • Calpain / chemistry
  • Calpain / drug effects
  • Calpain / genetics
  • Cysteine Endopeptidases / immunology
  • Cysteine Proteinase Inhibitors / pharmacology*
  • Dipeptides / pharmacology*
  • Drug Resistance
  • Glycoproteins / pharmacology
  • Leishmania / chemistry
  • Leishmania / physiology
  • Membrane Transport Proteins / drug effects*
  • Membrane Transport Proteins / genetics
  • Peptide Hydrolases / drug effects*
  • Peptide Hydrolases / genetics
  • Protozoan Proteins / immunology
  • Trypanosoma cruzi / chemistry
  • Trypanosoma cruzi / physiology
  • Trypanosomatina / drug effects*
  • Trypanosomatina / genetics

Substances

  • Cysteine Proteinase Inhibitors
  • Dipeptides
  • Glycoproteins
  • Membrane Transport Proteins
  • Protozoan Proteins
  • calpain inhibitors
  • Peptide Hydrolases
  • Calpain
  • Cysteine Endopeptidases
  • cruzipain
  • calpain inhibitor III