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 不同的细胞-细胞相互作用，包括口腔之间的 定植于牙齿上的放线菌和链球菌。半乳糖和N- 与2型菌毛相关的乙酰氨基半乳糖反应性凝集素 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菌株上的受体 S.sanguis、S.gordonii和S.mitis。抗原性可区分 多糖，每个由不同的，连接的磷酸二酯组成 重复的寡糖单元已被确定为受体分子 对3株口腔沙门氏菌、1株戈登氏沙门氏菌和2株沙门氏菌的研究 米氏链霉菌属(S.mitis)凝集素对这些多糖的识别发生在 每个寡糖重复单元的还原末端，取决于 普遍存在连接~16与Gal~13GalNAc`的内部半乳呋喃糖 或GalNAcbeta1至3Galpha。而放线菌(Actinmyces spp.)凝集素相互作用 对于含有任何一种受体结构的多糖，GalNAc- Gordonii等结合凝集素更喜欢GalNAcbeta1而不是 3Galpha-虽然某些半乳糖结合凝集素与Galbeta1反应最好 3含GalNAcalpha的多糖。猪瘟病毒的抗原性研究 这些多糖似乎取决于多糖的结构特征 不同于直接参与凝集素识别的重复单位。 这种功能区域的分离由 戈登氏链球菌38受体的结构和免疫化学性质 多糖类。该多糖的寡糖重复单元 具有结构上相同的非减径和减径端 米氏链霉菌J22和口腔链球菌34低聚糖分别为。 而菌株38多糖的抗原性与菌株38的抗原性相近 与菌株J22相似，菌株38的凝集素受体活性为 与34号菌株相似。