变形链球菌mutans表面蛋白P1对人唾液接受器研究

Study on the Human Salivary Acceptors of Streptococcus mutans MT_6R Surface Adhesin P1

收集人刺激性腮腺唾液，在碱性条件下聚丙烯酰胺凝胶电泳纯化唾液蛋白７种，命名为Ｂ１～Ｂ７，分别包被羟磷灰石珠，用１３１碘标记纯化的变形谜球菌ＭＴ６Ｒ（血清型ｃ）粘附素蛋白Ｐ１，观察其对每种唾液蛋白的粘附能力，以研究变形链珠菌粘附素蛋白Ｐ１的接受器。结果显示变形链球菌ｍｕｔａｎｓ表面蛋白Ｐ１对不同唾液蛋白的粘附量不同，具有选择性（Ｐ＜０．０１），对Ｂ５，Ｂ６粘附量特别高。已证实Ｂ５，Ｂ６为酸性富脯蛋白，提示酸性富脯蛋白可能为变形链球菌粘附素蛋白Ｐ１的重要接受器之一。

Abstract The human parotid saliva was separated by anionic polyacrylamide gel electrophoresis(PAGE)and seven bands of salivary proteins named B1～B7 were purified,in order to find out the acceptors of Streptococcus mutans MT6R(serotype c)adhesin P1,the adhesion of adhesin P1 labbelled with 131I(131 I-P1)to the different pellicles of seven purified salivary proteins were studied.The results showed that the 131I-P1 selectively adhere to the salivary protein components.The protein B5 was most effective in promoting attachment of 131I-P1 (P<0.01) and protein B5,protein B7 were less effective than protein B5,but more effective than the rest proteins(P<0.01).It has been demonstrated that protein B5 and B6 were the acidic proline-rich proteins.Therefore,acidic proline-rich proteins may be one of the most important acceptors of S.mutans MT6R(serotype c)adhesin P1.