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首页> 外文期刊>Infection and immunity >Classical complement pathway activation by antipneumococcal antibodies leads to covalent binding of C3b to antibody molecules.
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Classical complement pathway activation by antipneumococcal antibodies leads to covalent binding of C3b to antibody molecules.

机译：抗肺炎球菌抗体对经典补体途径的激活导致C3b与抗体分子共价结合。

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We have examined whether or not a physical relationship exists between antipneumococcal antibodies (Ab) and C3b when Ab activate the classical complement pathway on the surface of pneumococci (Pn). After sensitization with 125I-labeled Ab, Pn were sequentially incubated with purified C1, C4, C2, and biotinylated C3. Ab molecules were then eluted from Pn, and C3b-associated molecules were purified on avidin-Sepharose. Both 125I-labeled immunoglobulin G (IgG) and [125I]IgM bound to C3b; the association was stable to incubation in 1% sodium dodecyl sulfate at 37 degrees C. The association was only partially reversed by incubation in 1 M hydroxylamine-0.5% sodium dodecyl sulfate (pH 10.5), implying that Ab and C3b were linked by amide as well as ester bonds. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis of dithiothreitol and NH2OH eluates from the avidin-Sepharose showed that C3b bound to both heavy and light chains of the Ab. Moreover, the ability to bind to erythrocyte C3b receptors could be transferred to unsensitized Pn by eluates from Pn on which Ab had activated the classical pathway. These covalent complexes of Ab and C3b may be especially important in the opsonization of Pn by Ab and complement.
机译：我们已经检查了当Ab激活肺炎球菌（Pn）表面的经典补体途径时，抗肺炎球菌抗体（Ab）和C3b之间是否存在物理关系。用125 I标记的Ab致敏后，将Pn依次与纯化的C1，C4，C2和生物素化的C3孵育。然后从Pn中洗脱出Ab分子，并在抗生物素蛋白-Sepharose上纯化与C3b相关的分子。 125I标记的免疫球蛋白G（IgG）和[125I] IgM均与C3b结合;该缔合对于在37％的1％十二烷基硫酸钠中孵育是稳定的。通过在1 M羟胺-0.5％十二烷基硫酸钠（pH 10.5）中孵育，该缔合仅被部分逆转，这表明Ab和C3b通过酰胺连接以及酯键。二硫苏糖醇的十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和亲和素-Sepharose的NH2OH洗脱液显示C3b结合到Ab的重链和轻链上。此外，结合红细胞C3b受体的能力可以通过Ab激活经典途径的Pn洗脱液转移至未敏化的Pn。这些Ab和C3b的共价复合物在Ab和补体对Pn的调理作用中可能特别重要。

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