Ogier J A, Klein J P, Sommer P, Frank R M
Infect Immun. 1984 Jul;45(1):107-12. doi: 10.1128/iai.45.1.107-112.1984.
The ability of surface protein antigens of Streptococcus mutans to interact with salivary components was examined by Western blot and immunoprecipitation methods. Immunoblotting of S. mutans OMZ175 wall-associated antigens revealed 10 major antigens, designated according to their estimated molecular weights. Four of them, with molecular weights of 135,000, 125,000, 120,000, and 115,000 in their denaturated form, bound salivary components. This property was further investigated by immunoprecipitation experiments: the reactivity with saliva was confirmed for antigens with molecular weights of 135,000, 125,000, and 120,000 in their native form, and their locations on the bacterial cell surface were established. These three antigens were characterized as glycoproteins; they directly bound concanavalin A, and pronase abolished their antigenicity, which was partly retained after treatment with NaIO4. Because of their distribution in several other stains of S. mutans, it will be of interest to study their possible implication in the mechanism of attachment of streptococcal strains to saliva-coated tooth surfaces.
通过蛋白质免疫印迹法和免疫沉淀法检测了变形链球菌表面蛋白抗原与唾液成分相互作用的能力。对变形链球菌OMZ175壁相关抗原进行免疫印迹分析，发现了10种主要抗原，并根据其估计分子量进行命名。其中4种抗原，变性形式的分子量分别为135,000、125,000、120,000和115,000，可与唾液成分结合。通过免疫沉淀实验对这一特性进行了进一步研究：证实了天然形式下分子量为135,000、125,000和120,000的抗原与唾液具有反应性，并确定了它们在细菌细胞表面的位置。这三种抗原被鉴定为糖蛋白；它们可直接与伴刀豆球蛋白A结合，链霉蛋白酶可消除其抗原性，用高碘酸钠处理后部分抗原性得以保留。由于它们在变形链球菌的其他几种菌株中也有分布，因此研究它们在链球菌菌株附着于唾液包被的牙齿表面的机制中可能发挥的作用将具有重要意义。
