Jimenez-Ruiz Elena, Morlon-Guyot Juliette, Daher Wassim, Meissner Markus
Wellcome Trust Centre for Molecular Parasitology, Institute of Infection, Immunity & Inflammation, College of Medical, Veterinary and Life Sciences, Glasgow, Lanarkshire, United Kingdom.
Dynamique des Interactions Membranaires Normales et Pathologiques, UMR5235 CNRS, Université Montpellier, Montpellier, France.
Mol Biochem Parasitol. 2016 Sep-Oct;209(1-2):18-25. doi: 10.1016/j.molbiopara.2016.01.007. Epub 2016 Feb 1.
The phylum Apicomplexa comprises more than 5000 species including pathogens of clinical and economical importance. These obligate intracellular parasites possess a highly complex endomembrane system to build amongst others three morphologically distinct secretory organelles: rhoptries, micronemes and dense granules. Proteins released by these organelles are essential for invasion and hijacking of the host cell. Due to the complexity of the internal organization of these parasites, a wide panoply of trafficking factors was expected to be required for the correct sorting of proteins towards the various organelles. However, Toxoplasma gondii and other apicomplexan parasites contain only a core set of these factors and several of the vacuolar protein sorting (VPS) homologues found in most eukaryotes have been lost in this phylum. In this review, we will summarise our current knowledge about the role of trafficking complexes in T. gondii, highlighting recent studies focused on complexes formed by VPS proteins. We also present a novel, hypothetical model, suggesting the recycling of parasite membrane and micronemal proteins.
顶复门包含5000多种物种，其中包括具有临床和经济重要性的病原体。这些专性细胞内寄生虫拥有高度复杂的内膜系统，可构建三种形态不同的分泌细胞器：棒状体、微线体和致密颗粒。这些细胞器释放的蛋白质对于入侵和劫持宿主细胞至关重要。由于这些寄生虫内部组织的复杂性，预计需要大量的运输因子才能将蛋白质正确分选到各种细胞器中。然而，弓形虫和其他顶复门寄生虫仅含有这些因子的核心集，并且大多数真核生物中发现的几种液泡蛋白分选（VPS）同源物在该门中已经丢失。在这篇综述中，我们将总结目前关于运输复合物在弓形虫中的作用的知识，重点介绍最近关于VPS蛋白形成的复合物的研究。我们还提出了一个新的假设模型，表明寄生虫膜和微线体蛋白的循环利用。
