Interaction of lysozyme with a surface protein antigen ofStreptococcus mutans

Abstract

The interaction of salivary lysozyme with the surface protein antigen (PAc) of Streptococcus mutans and the interaction of lysozyme with the pathogen were examined by ELISA using S. mutans MT8148 (PAc+) and the PAc-defective mutant EM-2 (PAc-). The lysozyme clearly bound to the S. mutans wild type but not to the S. mutans mutant. Furthermore, lysozyme bound directly in the fluid phase to the rPAc, of which the binding kinetics were determined (Kon = 3.63 +/- 0.04 x 10(3) M-1 s-1, K(off) = 1.72 +/- 0.04 x 10-5 s-1 and Kon/K(off) = 2.11 x 10(8) M-1) using surface plasmon resonance. The kinetics of both association and dissociation were relatively slow. In addition, anti-lysozyme antibody significantly inhibited the binding of salivary components to the rPAc. The present findings indicate that lysozyme is one of the major salivary components interacting with S. mutans PAc.

Antibacterial and Antibiofilm Photodynamic Activities of Lysozyme-Au Nanoclusters/Rose Bengal Conjugates

“…However, the interaction of Lys with S. mutans has been demonstrated previously . Such an interaction is also expected for Lys-Au NCs/RB and S.…”

“…35 However, the interaction of Lys with S. mutans has been demonstrated previously. 36 Such an interaction is also expected for Lys-Au NCs/RB and S. mutans, which may enhance aPDT action on S. mutans. Investigation of the interactions between Lys-Au NCs/RB and S. mutans would be informative but are beyond the scope of this investigation.…”

Enhancement of Ligand Immobilization on Gold Surface by Optimizing Monolayer Concentration and Pre‐Concentration Studies for Surface Plasmon Resonance Analysis of Rutin‐Lysozyme Interaction

“…The K a and K d values were determined to be 3.63 � 0.03×10 3 M À 1 s À 1 and 1.72 � 0.04×10 À 5 s À 1 , respectively. [54] In this study, several parameters were optimized to obtain ideal SPR binding data. Based on the results regarding the effect of buffer type and pH on ligand immobilization, phosphate buffer (pH 7.5) proved to be useful as coupling buffer for optimum ligand immobilization.…”