UV-triggered affinity capture identifies interactions between the Plasmodium falciparum multidrug resistance protein 1 (PfMDR1) and antimalarial agents in live parasitized cells

J Biol Chem. 2013 Aug 2;288(31):22576-83. doi: 10.1074/jbc.M113.453159. Epub 2013 Jun 10.

Abstract

A representative of a new class of potent antimalarials with an unknown mode of action was recently described. To identify the molecular target of this class of antimalarials, we employed a photo-reactive affinity capture method to find parasite proteins specifically interacting with the capture compound in living parasitized cells. The capture reagent retained the antimalarial properties of the parent molecule (ACT-213615) and accumulated within parasites. We identified several proteins interacting with the capture compound and established a functional interaction between ACT-213615 and PfMDR1. We surmise that PfMDR1 may play a role in the antimalarial activity of the piperazine-containing compound ACT-213615.

Keywords: ACT-213615; Affinity Capture; Drug Action; Mode of Action; Multidrug Transporters; PfMDR1; Photoaffinity Labeling; Plasmodium; Protein Drug Interactions.

Publication types

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

MeSH terms

  • ATP Binding Cassette Transporter, Subfamily B, Member 1 / physiology*
  • Animals
  • Antimalarials / pharmacology*
  • Plasmodium falciparum / physiology*
  • Ultraviolet Rays*

Substances

  • ATP Binding Cassette Transporter, Subfamily B, Member 1
  • Antimalarials