MICROBIAL ANTIGENS ASSOCIATED WITH SPECIFIC ADHERENCE

与特异性粘附相关的微生物抗原

• 批准号: 3854182
• 负责人: J O CISAR
• 金额: --
• 依托单位: NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH
• 依托单位国家: 美国
• 资助国家: 美国
• 起止时间: 至
• 项目状态: 未结题
• 来源: https://reporter.nih.gov/project-details/3854182
• 关键词: Actinomyces; adhesin; bacterial antigens; bacterial polysaccharides; bacterial proteins; cell adhesion; dental caries; dental plaque; genetic strain; glycolipids; glycoproteins; gram negative bacteria; host organism interaction; microorganism immunology; molecular pathology; oligosaccharides; oral bacteria; pilus; saliva; surface antigens

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.

已知凝集素-碳水化合物结合在许多方面发挥着重要作用。 不同细胞与细胞之间的相互作用，包括口腔之间的相互作用 定植于牙齿的放线菌和链球菌。 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的结合互补 大多数口腔链球菌分离株以及某些菌株上的受体 S. sanguis、S. gordonii 和 S. mitis。 抗原性可区分 多糖，每种都由不同的磷酸二酯连接组成 重复寡糖单元已被鉴定为受体分子 对三种口腔链球菌菌株、一种戈登链球菌菌株和两种菌株 S. mitis。 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取决于 内部呋喃半乳糖普遍存在，与 ~16 与 Gal~13GalNAc` 连接 或 GalNAcbeta1 至 3Galalpha。 而放线菌属。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（例如 S. gordonii 的凝集素）更喜欢 GalNAcbeta1 3Galalpha-而某些 Gal 结合凝集素与 Galbeta1 反应最好 含有 3GalNAcalpha 的多糖。 的抗原特性 这些多糖似乎取决于 除直接参与凝集素识别的重复单元外。 这种功能区域的分离通过 S. gordonii 38 受体的结构和免疫化学特性 多糖。 该多糖的寡糖重复单元 具有结构相同的非还原端和还原端 分别是 S. mitis J22 和 S.oralis 34 寡糖的那些。 而菌株38多糖的抗原特性密切相关 与菌株 J22 类似，菌株 38 凝集素受体活性为 与菌株34相似。