Molecular Helminthology Laboratory, Department of Infectious Disease and Global Health, Cummings School of Veterinary Medicine, Tufts University , North Grafton, MA , USA.
PeerJ. 2014 Mar 18;2:e316. doi: 10.7717/peerj.316. eCollection 2014.
Schistosomes are parasitic worms that can survive in the hostile environment of the human bloodstream where they appear refractory to both immune elimination and thrombus formation. We hypothesize that parasite migration in the bloodstream can stress the vascular endothelium causing this tissue to release chemicals alerting responsive host cells to the stress. Such chemicals are called damage associated molecular patterns (DAMPs) and among the most potent is the proinflammatory mediator, adenosine triphosphate (ATP). Furthermore, the ATP derivative ADP is a pro-thrombotic molecule that acts as a strong activator of platelets. Schistosomes are reported to possess at their host interactive tegumental surface a series of enzymes that could, like their homologs in mammals, degrade extracellular ATP and ADP. These are alkaline phosphatase (SmAP), phosphodiesterase (SmNPP-5) and ATP diphosphohydrolase (SmATPDase1). In this work we employ RNAi to knock down expression of the genes encoding these enzymes in the intravascular life stages of the parasite. We then compare the abilities of these parasites to degrade exogenously added ATP and ADP. We find that only SmATPDase1-suppressed parasites are significantly impaired in their ability to degrade these nucleotides. Suppression of SmAP or SmNPP-5 does not appreciably affect the worms' ability to catabolize ATP or ADP. These findings are confirmed by the functional characterization of the enzymatically active, full-length recombinant SmATPDase1 expressed in CHO-S cells. The enzyme is a true apyrase; SmATPDase1 degrades ATP and ADP in a cation dependent manner. Optimal activity is seen at alkaline pH. The Km of SmATPDase1 for ATP is 0.4 ± 0.02 mM and for ADP, 0.252 ± 0.02 mM. The results confirm the role of tegumental SmATPDase1 in the degradation of the exogenous pro-inflammatory and pro-thrombotic nucleotides ATP and ADP by live intravascular stages of the parasite. By degrading host inflammatory signals like ATP, and pro-thrombotic signals like ADP, these parasite enzymes may minimize host immune responses, inhibit blood coagulation and promote schistosome survival.
血吸虫是一种寄生在人体血液中的寄生虫,它们能够在恶劣的环境中生存,对免疫清除和血栓形成都具有抵抗力。我们假设寄生虫在血液中的迁移可能会对血管内皮造成压力,导致这种组织释放化学物质,提醒相应的宿主细胞注意这种压力。这种化学物质被称为损伤相关分子模式(DAMPs),其中最有效的是促炎介质三磷酸腺苷(ATP)。此外,ATP 的衍生物二磷酸腺苷(ADP)是一种促血栓形成的分子,它是血小板的强激活剂。据报道,血吸虫在其与宿主相互作用的表皮表面拥有一系列的酶,这些酶可能与哺乳动物中的同源物一样,降解细胞外的 ATP 和 ADP。这些酶包括碱性磷酸酶(SmAP)、磷酸二酯酶(SmNPP-5)和三磷酸腺苷二磷酸水解酶(SmATPDase1)。在这项工作中,我们利用 RNAi 敲低寄生虫血管内生活阶段编码这些酶的基因的表达。然后,我们比较这些寄生虫降解外源性添加的 ATP 和 ADP 的能力。我们发现,只有抑制 SmATPDase1 的寄生虫在降解这些核苷酸的能力上受到显著影响。抑制 SmAP 或 SmNPP-5 不会显著影响蠕虫对 ATP 或 ADP 的代谢能力。这些发现通过在 CHO-S 细胞中表达具有酶活性的全长重组 SmATPDase1 得到了功能验证。该酶是一种真正的 apyrase;SmATPDase1 以依赖阳离子的方式降解 ATP 和 ADP。在碱性 pH 值下,酶的活性最佳。SmATPDase1 对 ATP 的 Km 值为 0.4 ± 0.02 mM,对 ADP 的 Km 值为 0.252 ± 0.02 mM。结果证实了表皮 SmATPDase1 在降解寄生虫血管内生活阶段的外源性促炎和促血栓形成核苷酸 ATP 和 ADP 中的作用。通过降解宿主的炎症信号,如 ATP,以及促血栓形成的信号,如 ADP,这些寄生虫酶可能会最小化宿主的免疫反应,抑制血液凝固,促进血吸虫的存活。