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溶组织内阿米巴介导的人类细胞外基质降解。

Invadosome-Mediated Human Extracellular Matrix Degradation by Entamoeba histolytica.

机构信息

Department of Medicine, University of Vermont Larner College of Medicine, Burlington, Vermont, USA.

Cellular, Molecular, and Biomedical Sciences Graduate Program, University of Vermont, Burlington, Vermont, USA.

出版信息

Infect Immun. 2018 Aug 22;86(9). doi: 10.1128/IAI.00287-18. Print 2018 Sep.

Abstract

is a protozoan parasite that causes invasive amoebiasis when it invades the human colon. Tissue invasion requires a shift from an adhesive lifestyle in the colonic lumen to a motile and extracellular matrix (ECM) degradative lifestyle in the colonic tissue layers. How the parasite regulates these two lifestyles is largely unknown. Previously, we showed that silencing the surface metalloprotease EhMSP-1 results in parasites that are hyperadherent and less motile. To better understand the molecular mechanism of this phenotype, we now show that the parasites with silenced cannot efficiently form specialized dot-like polymerized actin (F actin) structures upon interaction with the human ECM component fibronectin. We characterized these F actin structures and found that they are very short-lived structures that are the sites of fibronectin degradation. Motile mammalian cells form F actin structures called invadosomes that are similar in stability and function to these amoebic actin dots. Therefore, we propose here that forms amoebic invadosomes to facilitate colonic tissue invasion.

摘要

是一种原生动物寄生虫,当它侵入人体结肠时会引起侵袭性阿米巴病。组织入侵需要从在结肠腔中的粘附生活方式转变为在结肠组织层中的运动和细胞外基质(ECM)降解生活方式。寄生虫如何调节这两种生活方式在很大程度上是未知的。以前,我们表明,沉默表面金属蛋白酶 EhMSP-1 会导致寄生虫过度粘附和运动能力降低。为了更好地理解这种表型的分子机制,我们现在表明,沉默的寄生虫在与人类 ECM 成分纤连蛋白相互作用时不能有效地形成特殊的点状聚合肌动蛋白(F 肌动蛋白)结构。我们对这些 F 肌动蛋白结构进行了表征,发现它们是非常短暂的结构,是纤连蛋白降解的部位。运动的哺乳动物细胞形成 F 肌动蛋白结构,称为入侵小体,其稳定性和功能与这些阿米巴肌动蛋白点相似。因此,我们在这里提出,形成阿米巴入侵小体以促进结肠组织入侵。

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