Isolation and characterization of a 180-kiloDalton salivary glycoprotein which mediates the attachment of Actinomyces naeslundii to human buccal epithelial cells.
Isolation and characterization of a 180-kiloDalton salivary glycoprotein which mediates the attachment of Actinomyces naeslundii to human buccal epithelial cells.
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180 千道尔顿唾液糖蛋白的分离和表征，该糖蛋白介导内氏放线菌与人口腔上皮细胞的附着。
DOI：
10.1111/j.1600-0765.1991.tb01632.x
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发表时间：
1991
影响因子：
3.5
通讯作者：
Abraham,SN
中科院分区：
文献类型：
--
作者：
Babu,JP;Dabbous,MK;Abraham,SN
内斯伦迪放线菌对人颊粘膜的粘附是由细菌细胞表面菌毛与上皮细胞表面互补的β-连接半乳糖苷受体之间的特异性相互作用介导的。口腔粘膜和在其表面定居的细菌不断地沐浴在唾液中。一些唾液成分被认为在调节口腔细菌和颊上皮之间的粘附相互作用中起重要作用。我们已经观察到，用人腮腺唾液预处理分离的颊上皮细胞（BEC）增加了三种不同菌株的A。内氏菌。通过采用亲和色谱、离子交换和高压液相色谱技术，我们分离出了180 kDaA。内氏结合唾液糖蛋白（An-SGP）。这种唾液糖蛋白能够介导与A. Naeslundii和BEC.用增加量的An-SGP预处理BEC导致A的附着相应增加。内氏菌。A. An-SGP-包被的BEC对先前显示的阻断A粘附的相同抑制剂敏感。Naeslundiito未包被的BEC，即乳糖和半乳糖基结合凝集素。当新鲜分离和洗涤的BEC的溶解提取物在Western印迹上与An-SGP抗体反应时，检测到显著的180 kDa免疫反应性条带。此外，当使用An-SGP-特异性抗体通过免疫荧光测定时，在BEC表面上证明了免疫反应性组分，表明BEC上存在An-SGP或与分离的糖蛋白在结构和免疫学上相同的蛋白质。
The adherence ofActinomyces naeslundiito human buccal mucosa is mediated by specific interactions between the bacterial cell surface fimbriae and complementary β‐linked galactoside receptors on the epithelial cell surface. The buccal mucosa and the bacteria that colonize its surface are constantly bathed in saliva. Several salivary components are thought to play an important role in modulating adhesive interactions between oral bacteria and the buccal epithelium. We have observed that pretreatment of isolated buccal epithelial cells (BEC) with human parotid saliva increased the attachment of three different strains ofA. naeslundii. By employing affinity chromatography, ion‐exchange and high‐pressure liquid Chromatographic techniques we have isolated a 180 kDaA. naeslundii‐binding salivary glycoprotein (An‐SGP). This salivary glycoprotein was capable of mediating separate but specific binding interactions withA. naeslundiiand BEC. Pretreatment of BEC with increasing amounts of An‐SGP resulted in a corresponding increase in the attachment ofA. naeslundii. The adherence ofA. naeslundiito An‐SGP‐coated BEC is sensitive to the same inhibitors previously shown to block adherence ofA. naeslundiito uncoated BEC, namely lactose and galactosyl‐binding lectins. When a solubilized extract of freshly isolated and washed BEC was reacted on a Western blot with antibodies to An‐SGP, a prominent 180 kDa immunoreactive band was detected. Furthermore, the immunoreactive component was demonstrated on the BEC surface when assayed by immunofluorescence using An‐SGP‐specific antibodies, suggesting that An‐SGP or a protein structurally and immunologically identical to the isolated glycoprotein is present on BEC.