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Attenuation of Glucan-binding Protein C Reduces the Cariogenicity of Streptococcus mutans: Analysis of Strains Isolated from Human Blood

K. Nakano1, M. Matsumura1, M. Kawaguchi1, T. Fujiwara1, S. Sobue1, I. Nakagawa2, S. Hamada2, and T. Ooshima1,*

1 Departments of Pedodontics and
2 Oral Microbiology, Osaka University Graduate School of Dentistry, 1-8 Yamada-oka, Suita, Osaka 565-0871, Japan;



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Figure 1. Cellular adhesion and dextran-binding activities of TW strains and MT8148 (mean ± SD; n = 5). (A) Sucrose-independent cellular adhesion to saliva-coated hydroxyapatite of MT8148, GbpC-defective mutant (C1), and TW strains. (B) Dextran-binding activity of MT8148, C1, and TW strains. There were statistically significant differences between MT8148 and the other strains by Fisher's PLSD analysis. (**P < 0.01, ***P < 0.001).

 


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Figure 2. Identification of gbpA, gbpC, and expressed GbpC. Southern hybridization analyses of S. mutans gbpA (A) and gbpC (B), and Western blot analysis of GbpC (C), among MT8148 and TW strains. The arrows indicate GbpC of each strain. Lanes: 1, MT8148; 2, C1; 3, TW871; and 4, TW964.

 


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Figure 3. Putative structure of GpbC of TW strains and MT8148. (A) Map of putative nucleotide structure of gbpC among MT8148 and TW strains. A base pair (BP) scale is illustrated above the map. Cell wall anchored region. 39 amino acid deletions seen in TW871 strain. (B) C-terminus deduced amino acid alignment of GbpC of MT8148 and TW strains. 460-580 at the top of (B) indicates the serial number of deduced amino acids in MT8148.

 





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