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Separation of T-cell-stimulating activity from streptococcal M protein.

机译:T细胞刺激活性与链球菌M蛋白的分离。

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The superantigenic properties of M protein type 5 of Streptococcus pyogenes have been implicated as an important pathogenicity factor in streptococcal autoimmune diseases. Here we show that after a single purification step by affinity chromatography on immobilized albumin or fibrinogen, M protein has no mitogenic activity for T cells. We demonstrate that the superantigenicity of M proteins of type 5 and type 1 is due to contamination with the highly potent pyrogenic exotoxins of S. pyogenes in the range of 0.1 to 0.01%. These results raise a general caveat for work with these extremely active T-cell mitogens, because the mitogenicity of other streptococcal or staphylococcal proteins could be due to similar minute contamination with potent superantigens that are undetectable by any biochemical method but extremely effective in stimulating sensitive T cells.
机译:化脓性链球菌的M蛋白5型的超抗原性已被认为是链球菌自身免疫性疾病的重要致病因素。在这里,我们显示在固定化白蛋白或纤维蛋白原上通过亲和色谱法进行的单个纯化步骤后,M蛋白对T细胞没有促有丝分裂活性。我们证明类型5和类型1的M蛋白的超抗原性是由于化脓性链球菌的强效热原性外毒素在0.1%至0.01%范围内的污染所致。这些结果引起了对使用这些极活泼的T细胞丝裂原进行工作的普遍警告,因为其他链球菌或葡萄球菌蛋白质的有丝分裂性可能是由于强效超抗原受到类似的微小污染,而这些超抗原是任何生化方法都无法检测到的,但是对刺激敏感的T极为有效。细胞。

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