| abstract |
The development of dental plaque is inhibited by blocking bacteria/pellicle binding sites or by inhibiting the action of plaque-forming enzymes, in either case by means of a novel binding protein. A population of muteins is generated by extensive random mutagenesis of selected codons of a gene encoding a suitably stable protein, e.g., aprotonin. The muteins are expressed by a phage, bacterial cell or bacterial spore and displayed on its outer surface. Displayed muteins which bind to a pellicular protein, such as a proline-rich protein or statherin, or to a plaque-forming bacterial enzyme, such as a streptococcal glucosyltransferase, are isolated by affinity chromatography. The pellicle binding proteins may be used directly, or to tether a GTF inhibitor protein. |