title: [A study on the conjugation of Streptococcus mutans adhesins and its salivary receptors].
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.
  
  
  CONCLUSIONS
  The adhesion of S. mutans is a result of reaction between multireceptors and multiadhesins.
authors.affiliation: School of Stomatology, West China University of Medical Sciences, Chengdu 610041.
authors.forename: L
authors.initials: L
authors.lastname: Zhan
authors.forename: T
authors.initials: T
authors.lastname: Liu
authors.forename: M
authors.initials: M
authors.lastname: Fu
mesh_terms: D018829:Adhesins, Bacterial / Q000378:metabolism*; D001422:Bacterial Adhesion; D001667:Binding, Competitive; D006801:Humans; D011485:Protein Binding; D012463:Saliva / Q000378:metabolism*; D013295:Streptococcus mutans / Q000737:chemistry / Q000502:physiology*
chemical_list: D018829:Adhesins, Bacterial