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Roles of Salivary Proteins in the Adherence of Oral Streptococci to Various Orthodontic Brackets

S.-J. Ahn1, H.-S. Kho2, S.-W. Lee2, and D.-S. Nahm1,*

1 Department of Orthodontics, College of Dentistry, Seoul National University, 28-22 Yunkeun-Dong, Chongro-Ku, Seoul 110-744, Korea (ROK); and
2 Department of Oral Medicine and Oral Diagnosis, College of Dentistry, Seoul National University;



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  		Figure 1. SDS-PAGE (10%) of pellicles formed on orthodontic brackets. Lane 1, Unstimulated whole saliva; Lane 2, experimental bracket pellicle (EBP) formed on metal brackets; Lane 3, EBP on polycrystalline alumina brackets; Lane 4, EBP on monocrystalline sapphire brackets; and Lane 5, EBP on plastic brackets. The gel was stained with 0.25% Coomassie brilliant blue. Immunodetection of these components identified, the 13- to 20-kd molecule as cystatins, the 30-kd molecule as acidic proline-rich proteins, the 55-kd molecule as {alpha}-chain of sIgA, the 60-kd molecule as {alpha}-amylase, and the 120-kd molecule as low-molecular-weight mucin.

 


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  		Figure 2. Binding of 3H-labeled Streptococcus gordonii DL1 to salivary proteins on polyvinylidene fluoride (A) and nitrocellulose (B) membranes. Lane 1, unstimulated whole saliva; Lane 2, experimental bracket pellicle (EBP) formed on metal brackets; Lane 3, EBP on polycrystalline alumina brackets; Lane 4, EBP on monocrystalline sapphire brackets; and Lane 5, EBP on plastic brackets. Binding of S. gordonii was mediated by acidic proline-rich proteins, a 40-kd molecule, {alpha}-amylase, and low-molecular-weight mucin.

 




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