Calorimetric comparison of the interactions between salivary proteins and Streptococcus mutans with and without antigen I/II

C.P. Xu, B. van de Belt-Gritter, H.J. Busscher, H.C. van der Mei, W. Norde

Research output: Contribution to journalArticleAcademicpeer-review

10 Citations (Scopus)

Abstract

Antigen I/II can be found on streptococcal cell surfaces and is involved in their interaction with salivary proteins. In this paper, we determine the adsorption enthalpies of salivary proteins to Streptococcus mutans LT11 and S. mutans IB03987 with and without antigen I/II, respectively, using isothermal titration calorimetry. In addition, protein adsorption to the cell surfaces was determined spectrophotometrically. S. mutans LT11 with antigen I/II, yielded a much higher, exothermic adsorption enthalpy at pH 6.8 (ranging from ¿2073 × 10¿9 to ¿31707 × 10¿9 ¿J per bacterium) when mixed with saliva than did S. mutans IB03987 (¿165 × 10¿9 to ¿1107 × 10¿9 ¿J per bacterium) at all bacterial concentrations studied (5 × 109, 5 × 108, and 5 × 107 ml¿1), largest effects per bacterium being observed for the lowest concentration. However, the enthalpy of salivary protein adsorption to S. mutans LT11 became smaller at pH 5.8. Adsorption isotherms for the S. mutans LT11 showed considerable protein adsorption at pH 6.8 (1.2¿2.1 mg/m2), that decreased only slightly at pH 5.8 (1.1¿1.6 mg/m2), with the largest amount adsorbed at the lowest bacterial concentration. This suggests that the protein(s) in the saliva with the strongest affinity for antigen I/II is (are) readily depleted from saliva. In conclusion, antigen I/II surface proteins on S. mutans play a determinant role in adsorption of salivary proteins through the creation of enthalpically favorable adsorption sites.
Original languageEnglish
Pages (from-to)193-199
JournalColloids and Surfaces. B: Biointerfaces
Volume54
Issue number2
DOIs
Publication statusPublished - 2007

Keywords

  • surface protein
  • components
  • intermedius
  • adsorption
  • receptors
  • strains
  • binding
  • systems

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