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Myosin II is involved in capping and uroid formation in the human pathogen Entamoeba histolytica.

机译:肌球蛋白II参与人类病原体Entamoeba histolytica的加帽和尿酸形成。

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The redistribution and capping of surface receptors on the human pathogen Entamoeba histolytica was observed in the presence of concanavalin A (ConA). Capping was correlated with plasma membrane folding towards the rear of the amoeba and with uroid formation. The uroid is thought to play a role in the escape of amoebae from the host immune response. To localize myosin II during capping, amoebae were incubated in the presence of ConA and then analyzed by microscopy. Myosin II was three times more concentrated within the uroid compared with the rest of the cell, suggesting that the release of caps may depend upon mechanical contraction driven by myosin II activity. The use of drugs that disrupt cytoskeletal structure or that inhibit myosin heavy chain phosphorylation demonstrated that inhibition of capping prevents uroid formation. Biochemical analysis allowed the identification of two ConA receptors which have been previously described as major pathogenic antigens of this parasite: the 96-kDa antigen, which carries alcohol dehydrogenase 2 activity and binds extracellular matrix proteins, and the Gal-GalNAc-inhibitable surface lectin, which is involved in amoeba-cell interactions and in the degradation of complement particles attached to the parasite.
机译:在伴刀豆球蛋白A(ConA)的存在下,观察到人类病原体Entamoeba histolytica上表面受体的重新分布和封闭。封盖与质膜向变形虫后部的折叠以及与尿酸的形成有关。人们认为,类固醇在变形虫逃逸宿主免疫反应中起作用。为了在加帽过程中定位肌球蛋白II,将变形虫在ConA存在下孵育,然后通过显微镜进行分析。与细胞其余部分相比,肌球蛋白II在尿道内的浓度高出三倍,这表明帽的释放可能取决于肌球蛋白II活性驱动的机械收缩。破坏细胞骨架结构或抑制肌球蛋白重链磷酸化的药物的使用表明,抑制加帽可防止尿酸形成。生化分析可以鉴定出两个ConA受体,这些受体先前已被描述为该寄生虫的主要致病性抗原:96 kDa抗原,具有乙醇脱氢酶2活性并结合细胞外基质蛋白,以及Gal-GalNAc抑制性表面凝集素,这与变形虫细胞相互作用以及与寄生虫附着的补体颗粒的降解有关。

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