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葡萄球菌蛋白A的促有丝分裂活性归因于污染的葡萄球菌肠毒素。

Mitogenic activity of staphylococcal protein A is due to contaminating staphylococcal enterotoxins.

作者信息

Schrezenmeier H, Fleischer B

机构信息

Department of Medical Microbiology and Immunology, University of Ulm, F.R.G.

出版信息

J Immunol Methods. 1987 Dec 4;105(1):133-7. doi: 10.1016/0022-1759(87)90423-6.

Abstract

Soluble protein A from S. aureus is widely used as a polyclonal activator of human T cells. However, recombinant protein A produced in E. coli does not show any mitogenic properties, although its IgG-binding activity is identical to protein A purified from S. aureus. Antisera against the staphylococcal enterotoxins A and B are able to specifically inhibit the response of human T lymphocytes to protein A from S. aureus. Therefore, the mitogenic principle of this extensively used T cells activator is due to minute contaminations by enterotoxins that are active in picomolar concentrations.

摘要

来自金黄色葡萄球菌的可溶性蛋白A被广泛用作人T细胞的多克隆激活剂。然而,在大肠杆菌中产生的重组蛋白A不显示任何促有丝分裂特性,尽管其IgG结合活性与从金黄色葡萄球菌纯化的蛋白A相同。抗葡萄球菌肠毒素A和B的抗血清能够特异性抑制人T淋巴细胞对来自金黄色葡萄球菌的蛋白A的反应。因此,这种广泛使用的T细胞激活剂的促有丝分裂原理是由于皮摩尔浓度下具有活性的肠毒素的微量污染。

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