Richards Sashika N, Nash Megan N, Baker Eileen S, Webster Michael W, Lehane Adele M, Shafik Sarah H, Martin Rowena E
Research School of Biology, Australian National University, Canberra, Australia.
PLoS Pathog. 2016 Jul 21;12(7):e1005725. doi: 10.1371/journal.ppat.1005725. eCollection 2016 Jul.
Mutations in the Plasmodium falciparum 'chloroquine resistance transporter' (PfCRT) confer resistance to chloroquine (CQ) and related antimalarials by enabling the protein to transport these drugs away from their targets within the parasite's digestive vacuole (DV). However, CQ resistance-conferring isoforms of PfCRT (PfCRTCQR) also render the parasite hypersensitive to a subset of structurally-diverse pharmacons. Moreover, mutations in PfCRTCQR that suppress the parasite's hypersensitivity to these molecules simultaneously reinstate its sensitivity to CQ and related drugs. We sought to understand these phenomena by characterizing the functions of PfCRTCQR isoforms that cause the parasite to become hypersensitive to the antimalarial quinine or the antiviral amantadine. We achieved this by measuring the abilities of these proteins to transport CQ, quinine, and amantadine when expressed in Xenopus oocytes and complemented this work with assays that detect the drug transport activity of PfCRT in its native environment within the parasite. Here we describe two mechanistic explanations for PfCRT-induced drug hypersensitivity. First, we show that quinine, which normally accumulates inside the DV and therewithin exerts its antimalarial effect, binds extremely tightly to the substrate-binding site of certain isoforms of PfCRTCQR. By doing so it likely blocks the normal physiological function of the protein, which is essential for the parasite's survival, and the drug thereby gains an additional killing effect. In the second scenario, we show that although amantadine also sequesters within the DV, the parasite's hypersensitivity to this drug arises from the PfCRTCQR-mediated transport of amantadine from the DV into the cytosol, where it can better access its antimalarial target. In both cases, the mutations that suppress hypersensitivity also abrogate the ability of PfCRTCQR to transport CQ, thus explaining why rescue from hypersensitivity restores the parasite's sensitivity to this antimalarial. These insights provide a foundation for understanding clinically-relevant observations of inverse drug susceptibilities in the malaria parasite.
恶性疟原虫“氯喹抗性转运蛋白”(PfCRT)的突变通过使该蛋白将这些药物从寄生虫消化液泡(DV)内的靶点转运走,从而赋予对氯喹(CQ)及相关抗疟药的抗性。然而,赋予CQ抗性的PfCRT异构体(PfCRTCQR)也使寄生虫对一部分结构多样的药物超敏。此外,PfCRTCQR中抑制寄生虫对这些分子超敏性的突变同时恢复了其对CQ及相关药物的敏感性。我们试图通过表征导致寄生虫对抗疟药奎宁或抗病毒药金刚烷胺超敏的PfCRTCQR异构体的功能来理解这些现象。我们通过测量这些蛋白在非洲爪蟾卵母细胞中表达时转运CQ、奎宁和金刚烷胺的能力来实现这一点,并用检测PfCRT在寄生虫体内天然环境中的药物转运活性的试验对这项工作进行补充。在此,我们描述了PfCRT诱导药物超敏的两种机制解释。首先,我们表明通常在DV内积累并在其中发挥抗疟作用的奎宁,与PfCRTCQR某些异构体的底物结合位点紧密结合。这样做可能会阻断该蛋白对寄生虫生存至关重要的正常生理功能,从而使药物获得额外的杀伤作用。在第二种情况下,我们表明尽管金刚烷胺也在DV内蓄积,但寄生虫对这种药物的超敏性源于PfCRTCQR介导的金刚烷胺从DV转运到胞质溶胶中,在那里它可以更好地作用于其抗疟靶点。在这两种情况下,抑制超敏性的突变也消除了PfCRTCQR转运CQ的能力,从而解释了为何从超敏状态恢复会使寄生虫对这种抗疟药恢复敏感性。这些见解为理解疟原虫临床上相关的反向药物敏感性观察结果奠定了基础。