SEPARATION OF T-CELL-STIMULATING ACTIVITY FROM STREPTOCOCCAL M-PROTEIN

被引：45

作者：

FLEISCHER, B ^{[1
]}

SCHMIDT, KH ^{[1
]}

GERLACH, D ^{[1
]}

KOHLER, W ^{[1
]}

机构：

[1] INST MICROBIOL & EXPTL THERAPY,O-6900 JENA,GERMANY

来源：

INFECTION AND IMMUNITY | 1992年 / 60卷 / 05期

关键词：

D O I：

10.1128/IAI.60.5.1767-1770.1992

中图分类号：

R392 [医学免疫学]; Q939.91 [免疫学];

学科分类号：

100102 ;

摘要：

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.

引用

页码：1767 / 1770

页数：4

共 21 条

[1]

ABE J, 1991, J IMMUNOL, V146, P2447

[2] PEPTIC DIGESTION OF STREPTOCOCCAL M PROTEIN .2. EXTRACTION OF M ANTIGEN FROM GROUP A STREPTOCOCCI WITH PEPSIN [J].