Perdomo Doranda, Manich Maria, Syan Sylvie, Olivo-Marin Jean-Christophe, Dufour Alexandre C, Guillén Nancy
Cell Biology of Parasitism Unit, Institut Pasteur, Paris, France.
INSERM U786, Paris, France.
Cell Microbiol. 2016 Aug;18(8):1134-52. doi: 10.1111/cmi.12576. Epub 2016 Feb 26.
The development of amoebiasis is influenced by the expression of the lysine and glutamic acid rich protein 1 (KERP1), a virulence factor involved in Entamoeba histolytica adherence to human cells. Up to date, it is unknown how the protein transits the parasite cytoplasm towards the plasma membrane, specially because this organism lacks a well-defined endoplasmic reticulum (ER) and Golgi apparatus. In this work we demonstrate that KERP1 is present at the cell surface and in intracellular vesicles which traffic in a pathway that is independent of the ER-Golgi anterograde transport. The intracellular displacement of vesicles enriched in KERP1 relies on the actin-rich cytoskeleton activities. KERP1 is also present in externalized vesicles deposited on the surface of human cells. We further report the interactome of KERP1 with its association to endomembrane components and lipids. The model for KERP1 traffic here proposed hints for the first time elements of the endocytic and exocytic paths of E. histolytica.
溶组织内阿米巴病的发展受富含赖氨酸和谷氨酸的蛋白1（KERP1）表达的影响，KERP1是一种参与溶组织内阿米巴黏附人细胞的毒力因子。迄今为止，尚不清楚该蛋白如何穿过寄生虫细胞质到达质膜，特别是因为这种生物体缺乏明确的内质网（ER）和高尔基体。在这项研究中，我们证明KERP1存在于细胞表面和细胞内囊泡中，这些囊泡通过一条独立于ER-高尔基体顺向转运的途径运输。富含KERP1的囊泡在细胞内的移位依赖于富含肌动蛋白的细胞骨架活动。KERP1也存在于沉积在人细胞表面的外化囊泡中。我们进一步报道了KERP1的相互作用组及其与内膜成分和脂质的关联。这里提出的KERP1运输模型首次揭示了溶组织内阿米巴内吞和外排途径的要素。
