Ortiz Diana, Guiguemde W Armand, Johnson Alex, Elya Carolyn, Anderson Johanna, Clark Julie, Connelly Michele, Yang Lei, Min Jaeki, Sato Yuko, Guy R Kiplin, Landfear Scott M
Department of Molecular Microbiology & Immunology, Oregon Health & Science University, Portland, OR, United States of America.
Department of Chemical Biology & Therapeutics, St. Jude Children's Research Hospital, Memphis, TN, United States of America.
PLoS One. 2015 Apr 20;10(4):e0123598. doi: 10.1371/journal.pone.0123598. eCollection 2015.
Development of resistance against current antimalarial drugs necessitates the search for novel drugs that interact with different targets and have distinct mechanisms of action. Malaria parasites depend upon high levels of glucose uptake followed by inefficient metabolic utilization via the glycolytic pathway, and the Plasmodium falciparum hexose transporter PfHT, which mediates uptake of glucose, has thus been recognized as a promising drug target. This transporter is highly divergent from mammalian hexose transporters, and it appears to be a permease that is essential for parasite viability in intra-erythrocytic, mosquito, and liver stages of the parasite life cycle. An assay was developed that is appropriate for high throughput screening against PfHT based upon heterologous expression of PfHT in Leishmania mexicana parasites that are null mutants for their endogenous hexose transporters. Screening of two focused libraries of antimalarial compounds identified two such compounds that are high potency selective inhibitors of PfHT compared to human GLUT1. Additionally, 7 other compounds were identified that are lower potency and lower specificity PfHT inhibitors but might nonetheless serve as starting points for identification of analogs with more selective properties. These results further support the potential of PfHT as a novel drug target.
对当前抗疟药物产生耐药性,使得寻找与不同靶点相互作用且作用机制独特的新型药物成为必要。疟原虫依赖高水平的葡萄糖摄取,随后通过糖酵解途径进行低效的代谢利用,而介导葡萄糖摄取的恶性疟原虫己糖转运蛋白PfHT,因此被认为是一个有前景的药物靶点。这种转运蛋白与哺乳动物的己糖转运蛋白高度不同,并且它似乎是一种通透酶,对于疟原虫生命周期中红细胞内、蚊子和肝脏阶段的寄生虫生存能力至关重要。基于PfHT在墨西哥利什曼原虫寄生虫中的异源表达,开发了一种适用于针对PfHT进行高通量筛选的检测方法,这些墨西哥利什曼原虫寄生虫是其内源己糖转运蛋白的无效突变体。对抗疟化合物的两个聚焦文库进行筛选,鉴定出两种这样的化合物,与人类GLUT1相比,它们是PfHT的高效选择性抑制剂。此外,还鉴定出另外7种化合物,它们是效力较低且特异性较低的PfHT抑制剂,但仍可能作为鉴定具有更具选择性的类似物的起点。这些结果进一步支持了PfHT作为新型药物靶点的潜力。