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目的调查口腔副溶血链球菌黏附蛋白Fap1糖基化相关基因产物Gap1、Gap2和Gap3的亚细胞定位,以及相关基因缺陷株的黏附能力改变情况。方法等位置换技术获得口腔副溶血链球菌黏附蛋白糖基化相关基因缺陷株gap1-、gap2-和gap3-,穿梭质粒构建该三种基因的补偿株,Western Blot检测Gap1、Gap2和Gap3在副溶血链球菌内的亚细胞定位;闪烁计数法检测gap1-、gap2-和gap3-对羟基磷灰石的黏附能力。结果 Gap1和Gap2被发现分布于所有亚细胞组分中,但主要集中于胞浆和胞膜内,而Gap3仅分布于胞浆和胞膜;体外黏附实验显示gap1-、gap2-和gap3-对羟基磷灰石的黏附能力显著下降。结论糖基化修饰对副溶血链球菌黏附蛋白Fap1的黏附功能至关重要;Gap1、Gap2和Gap3可能在Fap1糖基化修饰过程中协同作用,该协同作用发生在胞内环境。
Objective To investigate the subcellular localization of the Gap1, Gap2 and Gap3 glycoprotein related gene products of Streptococcus mutans adhesin protein Fap1, and to investigate the changes of the adhesion capacity of related gene defective strains. Gap1, Gap2 and Gap3 were detected by Western Blot in the presence of substitutions of Gap1, Gap2 and Gap3 Subcellular localization of hemolytic streptococcus; scintillation counting method to detect gap1-, gap2- and gap3-hydroxyapatite adhesion. Results Gap1 and Gap2 were found in all subcellular fractions, but mainly in the cytoplasm and plasma membrane while Gap3 only distributed in the cytoplasm and plasma membrane. In vitro adhesion experiments showed that gap1-, gap2- and gap3- Hydroxyapatite adhesion decreased significantly. Conclusion Glycosylation is crucial for the adhesion of Fap1 to Streptococcus parahaemolyticus. Gap1, Gap2 and Gap3 may play synergistic roles in the glycosylation of Fap1, and this synergistic effect occurs in the intracellular environment.