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  • Title: [A study on the conjugation of Streptococcus mutans adhesins and its salivary receptors].
    Author: Zhan L, Liu T, Fu M.
    Journal: Zhonghua Kou Qiang Yi Xue Za Zhi; 1999 Jan; 34(1):19-21. PubMed ID: 11776527.
    Abstract:
    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.
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