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Yeast-based high-throughput screen identifies plasmodium falciparum equilibrative nucleoside transporter 1 inhibitors that kill malaria parasites

  • I. J. Frame
  • , Roman Deniskin
  • , Alison Rinderspacher
  • , Francine Katz
  • , Shi Xian Deng
  • , Robyn D. Moir
  • , Sophie H. Adjalley
  • , Olivia Coburn-Flynn
  • , David A. Fidock
  • , Ian M. Willis
  • , Donald W. Landry
  • , Myles H. Akabas

Producción científica: Article › revisión exhaustiva

32 Citas (Scopus)

Resumen

Equilibrative transporters are potential drug targets; however, most functional assays involve radioactive substrate uptake that is unsuitable for high-throughput screens (HTS). We developed a robust yeast-based growth assay that is potentially applicable to many equilibrative transporters. As proof of principle, we applied our approach to Equilibrative Nucleoside Transporter 1 of the malarial parasite Plasmodium falciparum (PfENT1). PfENT1 inhibitors might serve as novel antimalarial drugs since PfENT1-mediated purine import is essential for parasite proliferation. To identify PfENT1 inhibitors, we screened 64560 compounds and identified 171 by their ability to rescue the growth of PfENT1-expressing fui1Δ yeast in the presence of a cytotoxic PfENT1 substrate, 5-fluorouridine (5-FUrd). In secondary assays, nine of the highest activity compounds inhibited PfENT1-dependent growth of a purine auxotrophic yeast strain with adenosine as the sole purine source (IC50 0.2-2 μM). These nine compounds completely blocked [3H]adenosine uptake into PfENT1-expressing yeast and erythrocyte-free trophozoite-stage parasites (IC50 5-50 nM), and inhibited chloroquine-sensitive and -resistant parasite proliferation (IC50 5-50 μM). Wild-type (WT) parasite IC50 values were up to 4-fold lower compared to PfENT1-knockout (pfent1Δ) parasites. pfent1Δ parasite killing showed a delayed-death phenotype not observed with WT. We infer that, in parasites, the compounds inhibit both PfENT1 and a secondary target with similar efficacy. The secondary target identity is unknown, but its existence may reduce the likelihood of parasites developing resistance to PfENT1 inhibitors. Our data support the hypothesis that blocking purine transport through PfENT1 may be a novel and compelling approach for antimalarial drug development.

Idioma originalEnglish
Páginas (desde-hasta)775-783
Número de páginas9
PublicaciónACS Chemical Biology
Volumen10
N.º3
DOI
EstadoPublished - mar 20 2015

Nota bibliográfica

Publisher Copyright:
© 2015 American Chemical Society.

Financiación

FinanciadoresNúmero del financiador
National Institutes of Health (NIH)R01GM085177, R01AI116665
National Institute of Allergy and Infectious F32-AI286447 Cydney N. Johnson Diseases National Institute of Allergy and Infectious R01AI168214 Jason W. Rosch Diseases National Institute of Allergy and Infectious P30 Cydney N. Johnson Diseases National Institute of Allergy and Infectious R00-AI166116 Christopher D. Radka Diseases National Institute of Allergy and Infectious T32-AI106700 Cydney N. Johnson Diseases National Institute of Allergy and Infectious R01AI192221 Jason W. Rosch Diseases National Inst...R01AI085584

    ODS de las Naciones Unidas

    Este resultado contribuye a los siguientes Objetivos de Desarrollo Sostenible

    1. Good health and well being
      Good health and well being

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Medicine

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