Selective Binding of Blood Group-Reactive Salivary Mucins by Streptococcus mutans and Other Oral Organisms
Selective Binding of Blood Group-Reactive Salivary Mucins by Streptococcus mutans and Other Oral Organisms
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变形链球菌和其他口腔生物对血型反应性唾液粘蛋白的选择性结合
DOI：
10.1128/iai.22.3.665-671.1978
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发表时间：
1978
影响因子：
3.1
通讯作者：
J. Qureshi
中科院分区：
文献类型：
--
作者：
R. Gibbons;J. Qureshi
对4个基因群5个血清型的变形链球菌菌株和5株变形链球菌菌株进行了比较。sanguis，S. mitis，S. salivarius、内氏放线菌（Actinomyces naeslundii）和A.粘滞的，被发现结合血型反应性（BGR）粘蛋白分离自整个人类唾液。所研究的细菌结合粘蛋白与血型A或B的反应性在相似的程度上，这表明负责A和B抗原决定簇的碳水化合物部分不参与。所研究的微生物似乎与BGR粘蛋白分子的不同部分结合，因为被给定口腔种属的细胞吸收的制剂不再含有与同源微生物结合的BGR分子，但仍含有与其他细菌不同程度结合的BGR组分。甚至在S.属于不同基因组和血清学类型的变异株。在粘蛋白制剂中无法检测到免疫球蛋白，向反应混合物中加入抗人免疫球蛋白A（伊加）、IgG或IgM血清不影响结合。用高碘酸盐或碘乙酸盐预处理的粘蛋白不再与S.变形杆菌H12细胞，这表明碳水化合物部分和巯基基团起着至关重要的作用。BGR粘蛋白结合不需要活跃的细胞代谢;然而，用高碘酸盐或热（100°C持续15分钟）预处理H12细胞减少了结合。用[14 C]异硫氰酸苯酯标记的粘蛋白似乎与S.变形链球菌H12细胞与未处理的粘蛋白结合;这种结合似乎也是特异性的，因为当与过量的链球菌孵育时，少于15%的标记物质结合。[14 C]苯异硫氰酸酯标记的粘蛋白的结合不受中性糖测试或c抗原，甘油磷壁酸，葡聚糖，或粗葡糖基转移酶的制剂。然而，结合被几种胺抑制。BGR唾液粘蛋白存在于覆盖牙齿的获得性表膜中;细菌选择性结合这些组分的能力表明它们可能作为参与细菌与牙齿附着的受体分子。
Strains of Streptococcus mutans of four genetic groups and five serotypes, and strains of S. sanguis, S. mitis, S. salivarius, Actinomyces naeslundii, and A. viscosus, were found to bind blood group-reactive (BGR) mucin isolated from whole human saliva. The bacteria studied bound mucins with blood type A or B reactivity to a similar extent, suggesting that the carbohydrate moieties responsible for the A and B antigenic determinants were not involved. The organisms studied appeared to bind different fractions of BGR mucin molecules because preparations absorbed with cells of a given oral species no longer contained BGR molecules which bound to homologous organisms but still possessed BGR components which bound to varying degrees to other bacteria. Differences were even noted among S. mutans strains belonging to different genetic groups and serological types. Immunoglobulins could not be detected in the mucin preparations, and addition of anti-human immunoglobulin A (IgA), IgG, or IgM serum to reaction mixtures did not affect binding. Mucin pretreated with periodate or iodoacetate no longer bound to S. mutans H12 cells, suggesting that carbohydrate moieties and sulfhydryl groups played an essential role. Active cell metabolism was not required for BGR mucin binding; however, pretreatment of H12 cells with periodate or heat (100°C for 15 min) reduced binding. Mucin labeled with [14C]phenyl isothiocyanate appeared to bind to S. mutans H12 cells comparably to untreated mucin; the binding also appeared to be specific because less than 15% of the labeled material became bound when incubated with an excess of streptococci. Binding of [14C]phenyl isothiocyanate-labeled mucin was not affected by neutral sugars tested or by preparations of c antigen, glycerol teichoic acid, dextran, or crude glucosyltransferase. However, binding was inhibited by several amines. BGR salivary mucins are present in the acquired pellicle covering teeth; the ability of bacteria to selectively bind such components suggest that they may serve as receptor molecules involved in the attachment of bacteria to teeth.