摘要
目的研究变形链球菌表面粘结素与唾液受体间的对应结合关系。方法采用３Ｈ标记的变形链球菌（简称变链）竞争性粘附抑制实验及自行设计的间接酶联免疫受体结合实验，检测纯化唾液受体与纯化变链表面粘结素间的结合特异性及其强度。结果唾液ＩｇＡ降解片段和相对分子质量为１３０００的酸性蛋白仅促进变链粘附，唾液淀粉酶具有促进粘附及抗粘附双重作用。相对分子质量为１２７０００的变链表面粘结素及ＧＴＦ组分分别可竞争抑制变链对ＩｇＡ降解片段及淀粉酶的粘附，蛋白质Ｐ１和相对分子质量为１１７０００的粘结素可同时竞争抑制变链对此二种唾液组分的粘附；间接酶联免疫受体结合实验表明各变链粘结素不与ＩｇＡ降解片段有效结合。
Objective To investigate the conjugation specificity of Streptococcus mutans' adhesins and their salivary receptors. Methods Include purified salivary receptor or adhesin competitive bacteria adhesion inhibition test and enzyme linked immuno receptor assay (ELIRA) on S. mutans WD9463A. Results Salivary amylases can both enhance and competitively inhibit the adhesion of the strain to HA, while IgA degraded fragments and MW=13 000 protein only promote its adhesion. P1 and a 117 000 surface protein of WD9463A both inhibit adhesion of the strain to IgA degraded fragments and salivary amylases. An 127 000 protein of WD9463A and a kind of GTFase inhibit its adhesion to IgA degraded fragments and salivary amylases respectively. No conjugation was found between IgA degraded fragments and the adhesins, while reaction between amylases and the adhesins had basically accordance with adhesion inhibition test. Conclusion The adhesion of S. mutans is a result of reaction between multireceptors and multiadhesins.
出处
《中华口腔医学杂志》
CAS
CSCD
北大核心
1999年第1期19-21,共3页
Chinese Journal of Stomatology
