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首页> 外文期刊>Infection and immunity >Immunochemical analysis of intact M protein secreted from cell wall-less streptococci.
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Immunochemical analysis of intact M protein secreted from cell wall-less streptococci.

机译：从无细胞壁链球菌分泌的完整M蛋白的免疫化学分析。

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M protein is a major virulence factor of group A streptococci, which provides these organisms with protection against phagocytosis in the absence of specific antibody. To gain insight into the nature of the native M-protein molecule, type 12 M protein was isolated and purified from the extracellular supernatants of a group A streptococcal L form and stabilized protoplasts. The intact purified M protein from both sources had a molecular weight of 58,000, as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. This is in contrast to the 32,0000-dalton molecule isolated from the parent type 12 organism by using a nonionic detergent. The purified secretory M protein removed opsonic antibodies from type 12 rabbit immune serum, as demonstrated by a bactericidal assay. Therefore, it appears that either previous nondestructive methods of M-protein isolation have not removed intact M protein from cell walls or part of the molecule is fragmented during its association with cell walls.
机译：M蛋白是A组链球菌的主要毒力因子，可在缺乏特异性抗体的情况下为这些生物提供抗吞噬作用的保护作用。为了深入了解天然M蛋白分子的性质，从A组链球菌L型和稳定的原生质体的细胞外上清液中分离并纯化了12 M型蛋白。通过十二烷基硫酸钠-聚丙烯酰胺凝胶电泳测定，来自两种来源的完整纯化的M蛋白的分子量为58,000。这与使用非离子去污剂从12型母体中分离出的32,0000道尔顿分子相反。如杀菌试验所示，纯化的分泌性M蛋白从12型兔免疫血清中去除了调理素抗体。因此，似乎以前的M蛋白分离的非破坏性方法尚未从细胞壁上去除完整的M蛋白，或者分子的一部分在与细胞壁结合时被片段化了。

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