Department of Biochemistry & Molecular Biology, Oregon Health & Science University, Portland, Oregon, United States of America.
Division of Biological Sciences, Pacific Northwest National Laboratory, Richland, Washington, United States of America.
PLoS Pathog. 2014 Feb 27;10(2):e1003938. doi: 10.1371/journal.ppat.1003938. eCollection 2014 Feb.
The ability of Leishmania to survive in their insect or mammalian host is dependent upon an ability to sense and adapt to changes in the microenvironment. However, little is known about the molecular mechanisms underlying the parasite response to environmental changes, such as nutrient availability. To elucidate nutrient stress response pathways in Leishmania donovani, we have used purine starvation as the paradigm. The salvage of purines from the host milieu is obligatory for parasite replication; nevertheless, purine-starved parasites can persist in culture without supplementary purine for over three months, indicating that the response to purine starvation is robust and engenders parasite survival under conditions of extreme scarcity. To understand metabolic reprogramming during purine starvation we have employed global approaches. Whole proteome comparisons between purine-starved and purine-replete parasites over a 6-48 h span have revealed a temporal and coordinated response to purine starvation. Purine transporters and enzymes involved in acquisition at the cell surface are upregulated within a few hours of purine removal from the media, while other key purine salvage components are upregulated later in the time-course and more modestly. After 48 h, the proteome of purine-starved parasites is extensively remodeled and adaptations to purine stress appear tailored to deal with both purine deprivation and general stress. To probe the molecular mechanisms affecting proteome remodeling in response to purine starvation, comparative RNA-seq analyses, qRT-PCR, and luciferase reporter assays were performed on purine-starved versus purine-replete parasites. While the regulation of a minority of proteins tracked with changes at the mRNA level, for many regulated proteins it appears that proteome remodeling during purine stress occurs primarily via translational and/or post-translational mechanisms.
利什曼原虫在昆虫或哺乳动物宿主体内生存的能力依赖于其感知和适应微环境变化的能力。然而,对于寄生虫对环境变化(如营养可用性)的反应的分子机制知之甚少。为了阐明利什曼原虫中的营养应激反应途径,我们使用嘌呤饥饿作为范例。从宿主环境中回收嘌呤对于寄生虫的复制是必需的;然而,嘌呤饥饿的寄生虫可以在没有补充嘌呤的情况下在培养物中持续存在超过三个月,这表明对嘌呤饥饿的反应是强大的,并在极端匮乏的条件下产生寄生虫的生存。为了了解嘌呤饥饿期间的代谢重编程,我们采用了全局方法。在嘌呤饥饿和嘌呤丰富的寄生虫之间进行的全蛋白质组比较,跨越了 6-48 小时的时间范围,揭示了对嘌呤饥饿的时间和协调的反应。嘌呤转运蛋白和涉及细胞表面获取的酶在从培养基中去除嘌呤后的几个小时内被上调,而其他关键的嘌呤回收成分在时间过程中被上调得更晚且适度。48 小时后,嘌呤饥饿的寄生虫的蛋白质组被广泛重塑,对嘌呤应激的适应似乎专门针对嘌呤剥夺和一般应激。为了探究影响嘌呤饥饿反应的蛋白质组重塑的分子机制,对嘌呤饥饿和嘌呤丰富的寄生虫进行了比较 RNA-seq 分析、qRT-PCR 和荧光素酶报告基因测定。虽然少数蛋白质的调节与 mRNA 水平的变化相吻合,但对于许多受调节的蛋白质,嘌呤应激期间的蛋白质组重塑似乎主要通过翻译和/或翻译后机制发生。