Abstract
The oral pathogen Streptococcus mutans expresses a surface protein, P1, which interacts with the salivary pellicle on the tooth surface or with fluid-phase saliva, resulting in bacterial adhesion or aggregation, respectively. P1 is a target of protective immunity. Its N-terminal region has been associated with adhesion and aggregation functions and contains epitopes recognized by efficacious antibodies. In this study, we used Bacillus subtilis, a gram-positive expression host, to produce a recombinant N-terminal polypeptide of P1 (P139-512) derived from the S. mutans strain UA159. Purified P139-512 reacted with an anti-full-length P1 antiserum as well as one raised against intact S. mutans cells, indicating preserved antigenicity. Immunization of mice with soluble and heat-denatured P139-512 induced antibodies that reacted specifically with native P1 on the surface of S. mutans cells. The anti-P139-512 antiserum was as effective at blocking saliva-mediated aggregation of S. mutans cells and better at blocking bacterial adhesion to saliva-coated plastic surfaces compared with the anti-full-length P1 antiserum. In addition, adsorption of the anti-P1 antiserum with P1 39-512 eliminated its ability to block the adhesion of S. mutans cells to abiotic surfaces. The present results indicate that P1 39-512, expressed and purified from a recombinant B. subtilis strain, maintains important immunological features of the native protein and represents an additional tool for the development of anticaries vaccines.
Original language | English (US) |
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Pages (from-to) | 131-142 |
Number of pages | 12 |
Journal | FEMS Immunology and Medical Microbiology |
Volume | 59 |
Issue number | 2 |
DOIs | |
State | Published - Jul 2010 |
Externally published | Yes |
Keywords
- Antibody responses
- Bacillus subtilis
- P1 protein
- Recombinant proteins
- Saliva-binding region
- Streptococcus mutans
ASJC Scopus subject areas
- Immunology and Allergy
- Microbiology
- Immunology
- Microbiology (medical)
- Infectious Diseases