Interaction of lysozyme with a surface protein antigen of Streptococcus 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 wi...

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Bibliographic Details
Published in:FEMS microbiology letters 1996-06, Vol.139 (2-3), p.195-201
Main Authors: Senpuku, Hidenobu, Kato, Hirohisa, Todoroki, Megumi, Hanada, Nobuhiro, Nisizawa, Tosiki
Format: Article
Language:English
Subjects:
Adult
Antibodies
Antigens
Antigens, Surface - metabolism
Association kinetic constant
Bacterial Adhesion - physiology
Bacterial Proteins - metabolism
Bacteriology
Binding
Biological and medical sciences
Biosensing Techniques
Defective mutant
Dissociation kinetic constant
Enzyme-Linked Immunosorbent Assay
Fundamental and applied biological sciences. Psychology
Humans
Kinetics
Lysozyme
Male
Microbiology
Muramidase - antagonists & inhibitors
Muramidase - metabolism
Muramidase - pharmacology
Mutation - physiology
Pathogenicity, virulence, toxins, bacteriocins, pyrogens, host-bacteria relations, miscellaneous strains
Protein Binding - physiology
Proteins
Saliva - enzymology
Streptococcus infections
Streptococcus mutans
Streptococcus mutans - immunology
Surface plasmon resonance
Surface protein antigen
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Summary: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 × 103M−1s−1, Koff= 1.72 ± 0.04 × 10−5s−1 and Kon / Koff= 2.11 × 108M−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.
ISSN:0378-1097
1574-6968
DOI:10.1111/j.1574-6968.1996.tb08202.x