MICROBIAL ANTIGENS ASSOCIATED WITH SPECIFIC ADHERENCE

已知凝集素-碳水化合物结合在许多疾病中起重要作用。 不同细胞间的相互作用，包括口腔 放线菌和链球菌在牙齿上繁殖。 半乳糖和N- 与2型菌毛相关的乙酰半乳糖胺反应性凝集素 粘性放线菌和内氏放线菌，结合互补 大多数口腔链球菌分离株以及一些 S. sanguis，S. gordonii和S.缓解。 抗原可区分的 多糖，每种多糖由不同的磷酸二酯连接 重复的寡糖单元已被确定为受体分子 对三株S. oralis、1株S.戈登氏菌和两株 色葡萄缓解。 这些多糖的凝集素识别发生在 每个寡糖重复单元的还原端，并取决于 常见的内部呋喃半乳糖连接~16至Gal~ 13 GalNAc ` 或GalNAc β 1至3Galalpha。 而放线菌属（Actinomyces spp.）凝集素相互作用 与含有任一类型受体结构的多糖，GalNAc- 结合凝集素，如S. gordonii更喜欢GalNAc β 1， 3Galalpha-而某些Gal-binding凝集素与Galbeta 1反应最好， 3含GalNA α的多糖。 的抗原特性 这些多糖似乎取决于 除了直接参与凝集素识别的那些重复单位。 功能区域的这种分离由图1清楚地示出。 的结构和免疫化学性质。Gordonii 38受体 多糖 这种多糖的寡糖重复单位 具有结构上相同的非缩径端和缩径端， S. mitis J22和S. oralis 34寡糖。 而菌株38多糖的抗原特性与菌株38多糖的抗原特性密切相关， 与菌株J22相似，菌株38的凝集素受体活性是 与菌株34相似。

Lectin-carbohydrate binding is known to play an important role in a number of different cell-cell interactions including those between the oral actinomyces and streptococci that colonize teeth. Galactose- and N- acetylgalactosamine reactive lectins associated with the type 2 fimbriae of Actinomyces viscosus and Actinomyces naeslundii, bind complementary receptors on most Streptococcus oralis isolates as well as some strains of S. sanguis, S. gordonii, and S. mitis. Antigenically distinguishable polysaccharides, each composed of a different, phosphodiester linked repeating oligosaccharide unit have been identified as receptor molecules on three strains of S. oralis, one strain of S. gordonii and two strains of S. mitis. Lectin recognition of these polysaccharides occurs at the reducing end of each oligosaccharide repeating unit and depends on the common presence of internal galactofuranose linked ~16 to Gal~13GalNAc` or GalNAcbeta1 to 3Galalpha. Whereas Actinomyces spp. lectins interact with polysaccharides containing either type of receptor structure, GalNAc- binding lectins such as those of S. gordonii prefer GalNAcbeta1 to 3Galalpha-while certain Gal-binding lectins react best with Galbeta1 to 3GalNAcalpha-containing polysaccharides. The antigenic properties of these polysaccharides appear to depend on structural features of the repeating unit other than those directly involved in lectin recognition. This separation of functional regions is clearly illustrated by the structural and immunochemical properties of the S. gordonii 38 receptor polysaccharide. The oligosaccharide repeating unit of this polysaccharide has non-reducing and reducing ends that are structurally identical to those of the S. mitis J22 and S. oralis 34 oligosaccharides, respectively. Whereas the antigenic properties of the strain 38 polysaccharide closely resemble those of strain J22, the strain 38 lectin receptor activity is similar to that of strain 34.