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首页> 外文期刊>Infection and immunity >Anthrax protective antigen interacts with a specific receptor on the surface of CHO-K1 cells.
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Anthrax protective antigen interacts with a specific receptor on the surface of CHO-K1 cells.

机译：炭疽保护性抗原与CHO-K1细胞表面的特定受体相互作用。

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摘要

The interaction of protective antigen (PA), a component of the anthrax toxin, with receptors on the Chinese hamster ovary cell line CHO-K1 was characterized. Protective antigen binding at 4 degrees C is highly specific, concentration dependent, saturable (Kd = 0.9 nM), and reversible. Scatchard analysis indicates the presence of a single class of PA binding sites at a concentration of 10,000 +/- 2,000 per cell. Pretreatment of cells with a number of different proteases strongly inhibits PA binding, suggesting that the receptor may be at least partially proteinaceous. Direct chemical cross-linking of radioiodinated PA to the cell surface results in the appearance of a major band exhibiting an apparent molecular mass of 170 kDa, as estimated by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The appearance of this band is completely inhibited by a 200-fold molar excess of unlabeled PA, indicating a high specificity for this interaction. Our results suggest that a cell surface protein(s) of 85 to 90 kDa is, or constitutes a portion of, a specific receptor for the PA.
机译：表征了炭疽毒素成分保护性抗原（PA）与中国仓鼠卵巢细胞系CHO-K1上的受体的相互作用。 4℃下的保护性抗原结合是高度特异性的，浓度依赖性的，可饱和的（Kd ＝ 0.9nM）并且是可逆的。斯卡查德分析表明存在单个类别的PA结合位点，浓度为每个细胞10,000 +/- 2,000。用许多不同的蛋白酶对细胞进行预处理会强烈抑制PA的结合，表明该受体可能至少部分是蛋白质。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳估计，放射性碘化的PA与细胞表面的直接化学交联导致出现主带，该主带表现出170 kDa的表观分子量。该条带的出现被200倍摩尔过量的未标记PA完全抑制，表明这种相互作用具有高度特异性。我们的结果表明，85至90 kDa的细胞表面蛋白是PA的特异受体或构成其一部分。

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