Forsgren A, Svedjelund A, Wigzell H
Eur J Immunol. 1976 Mar;6(3):207-13. doi: 10.1002/eji.1830060312.
Protein A from Staphylococcus aureus (SpA) is known to bind to the Fc region of most mammalian IgG classes. In the present article data are presented showing that SpA is a highly efficient mitogen for human peripheral B lymphocytes, with no detectable activity for T lymphocytes. In order to achieve optimal stimulating conditions SpA should be presented to the lymphocytes on an insoluble matrix, such as the SpA-positive bacteria themselves or SpA covalently attached to Sephadex or Sepharose beads. Using such conditions SpA is equivalent with regard to stimulatory capacity for B lymphocytes as phytohemagglutinin is for the human T lymphocytes. Specificity controls proved beyond doubt that SpA and not any other contaminating product is the B cell mitogen. It is concluded that SpA as an inducer of human B lymphocyte division might serve as a highly useful assay in the clinical assessment of B lymphocyte function. It should also be a suitable tool in the fine analysis of B lymphocyte activation via the specific interactions with surface IgG molecules.
已知来自金黄色葡萄球菌的A蛋白（SpA）可与大多数哺乳动物IgG类别的Fc区域结合。在本文中，呈现的数据表明SpA是人类外周血B淋巴细胞的高效有丝分裂原，对T淋巴细胞无明显活性。为了达到最佳刺激条件，应将SpA以不溶性基质的形式呈现给淋巴细胞，例如SpA阳性细菌本身或共价连接到葡聚糖凝胶或琼脂糖珠上的SpA。在这样的条件下，SpA对B淋巴细胞的刺激能力等同于植物血凝素对人类T淋巴细胞的刺激能力。特异性对照毫无疑问地证明是SpA而非任何其他污染产物是B细胞有丝分裂原。得出的结论是，SpA作为人类B淋巴细胞分裂的诱导剂，可能在B淋巴细胞功能的临床评估中作为一种非常有用的检测方法。它也应该是通过与表面IgG分子的特异性相互作用对B淋巴细胞活化进行精细分析的合适工具。
