Plasmodium falciparum chloroquine resistance transporter is a H+ -coupled polyspecific nutrient and drug exporter

Narinobu Juge, Sawako Moriyama, Takaaki Miyaji, Mamiyo Kawakami, Haruka Iwai, Tomoya Fukui, Nathan Nelson, Hiroshi Omote, Yoshinori Moriyama

Research output: Contribution to journalArticlepeer-review

47 Citations (Scopus)


Extrusion of chloroquine (CQ) from digestive vacuoles through the Plasmodium falciparum CQ resistance transporter (PfCRT) is essential to establish CQ resistance of the malaria parasite. However, the physiological relevance of PfCRT and how CQ-resistant PfCRT gains the ability to transport CQ remain unknown. We prepared proteoliposomes containing purified CQ-sensitive and CQ-resistant PfCRTs and measured their transport activities. All PfCRTs tested actively took up tetraethylammonium, verapamil, CQ, basic amino acids, polypeptides, and polyamines at the expense of an electrochemical proton gradient. CQ-resistant PfCRT exhibited decreased affinity for CQ, resulting in increased CQ uptake. Furthermore, CQ competitively inhibited amino acid transport. Thus, PfCRT is a H+-coupled polyspecific nutrient and drug exporter.

Original languageEnglish
Pages (from-to)3356-3361
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number11
Publication statusPublished - Mar 17 2015


  • Amino acid
  • Chloroquine
  • Malaria
  • Pfcrt
  • Transporter

ASJC Scopus subject areas

  • General


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