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细菌AB₅型肠毒素——结构、功能及作用机制

Bacterial type AB₅ enterotoxins--structure, function and mechanism of action.

作者信息

Komiażyk Magdalena, Palczewska Małgorzata, Pikula Sławomir, Groves Patrick

出版信息

Postepy Biochem. 2015;61(4):430-5.

Abstract

One of the main factors causing bacterial diarrhea are AB₅ enterotoxins. This group is divided into four families: pertussis toxin, cholera toxin, shiga toxin and subtilase cytotoxin. In this review we will describe the activity, structure and function of the cholera and shiga toxin families. The AB₅ enterotoxins contain a catalytic subunit A and pentameric subunit B, which binds to the cell surface within lipid rafts. The cholera toxin family cause the constitutive activation of Gsa protein, which results in cAMP production, an opening of the chloride channels and releases chloride ions into the lumen of the small intestine. In contrast, the shiga toxin family has a cytotoxic effect on epithelial cells. It can inhibit protein synthesis leading to cell death. Although AB₅ has a toxic activity, the B₅ subunits have a significant potential as a transporter for proteins with anticancer activity and as a tool for the visualization of lipid rafts and cancer cells.

摘要

导致细菌性腹泻的主要因素之一是AB₅肠毒素。该类毒素分为四个家族:百日咳毒素、霍乱毒素、志贺毒素和枯草杆菌蛋白酶细胞毒素。在本综述中,我们将描述霍乱毒素家族和志贺毒素家族的活性、结构与功能。AB₅肠毒素包含一个催化亚基A和一个五聚体亚基B,后者可在脂筏内与细胞表面结合。霍乱毒素家族会导致Gsa蛋白的组成性激活,从而产生环磷酸腺苷(cAMP),使氯离子通道开放,并将氯离子释放到小肠肠腔中。相比之下,志贺毒素家族对上皮细胞具有细胞毒性作用。它可抑制蛋白质合成,导致细胞死亡。尽管AB₅具有毒性活性,但B₅亚基作为具有抗癌活性蛋白质的转运体以及作为脂筏和癌细胞可视化工具具有巨大潜力。

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