Streptococcus sanguis may play an important role in the initiation and maturation of dental plaque. These bacteria are among the first to colonize tooth surfaces by binding to components of the acquired salivary pellicle and serve in turn as binding sites for subsequent adherence of several other plaque bacteria. This interbacterial colonization is characteristic of the succession of bacterial adherence seen during plaque maturation. It has also been proposed that coherence of S. sanguis with black-pigmenting Bacteroides may permit these gram negative bacteria to colonize the oral cavity and ultimately the periodontal pocket. The long- range objective of this project is to characterize the coaggregation between S. sanguis and B. gingivalis and to define the modulating effects of human saliva and serum components on this phenomenon. Selected strains of S. sanguis and B. gingivalis (stock strains and fresh clinical isolates) will be tested for their coaggregating activities using visual and radioactivity assays. The effects of unfractionated saliva and serum samples on bacterial coaggregation will be studied in these assay systems. Components of saliva and serum that either inhibit or enhance coaggregation will be identified for further study. Specifically, host components that bind to surface structures of streptococci or bacteroides will be extracted from the cells with sodium dodecyl sulfate and identified by Western Blot assays using libraries of polyclonal and monoclonal reagents. The active component will then be isolated from saliva or serum using chromotographic procedures and analyzed for its activity on bacterial coaggregation. The structural domains of the salivary molecule which mediate coaggregation will be ascertained by studying the effects of reduction and alkylation, deglycosylation, delipidation, dephosphorylation, and proteolytic degradation. Finally, salivary composite molecules (subproject I.A.) will be assayed for modulation of streptococcal and Bacteroides coaggregation activity. We anticipate that the information from these studies could provide a rationale for selectivity regulating bacterial succession.

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Specialized Center (P50)
Project #
5P50DE008240-04
Application #
3875384
Study Section
Project Start
Project End
Budget Start
Budget End
Support Year
4
Fiscal Year
1990
Total Cost
Indirect Cost
Name
State University of New York at Buffalo
Department
Type
DUNS #
038633251
City
Buffalo
State
NY
Country
United States
Zip Code
14260
Ohkusa, Toshifumi; Yoshida, Tsutomu; Sato, Nobuhiro et al. (2009) Commensal bacteria can enter colonic epithelial cells and induce proinflammatory cytokine secretion: a possible pathogenic mechanism of ulcerative colitis. J Med Microbiol 58:535-45
Sojar, Hakimuddin T; Genco, Robert J (2005) Identification of glyceraldehyde-3-phosphate dehydrogenase of epithelial cells as a second molecule that binds to Porphyromonas gingivalis fimbriae. FEMS Immunol Med Microbiol 45:25-30
Satyanarayana, J; Gururaja, T L; Narasimhamurthy, S et al. (2001) Synthesis and conformational features of human salivary mucin C-terminal derived peptide epitope carrying Thomsen-Friedenreich antigen: implications for its role in self-association. Biopolymers 58:500-10
Narasimhamurthy, S; Naganagowda, G A; Janagani, S et al. (2000) Solution structure of O-glycosylated C-terminal leucine zipper domain of human salivary mucin (MUC7). J Biomol Struct Dyn 18:145-54
Gururaja, T L; Levine, J H; Tran, D T et al. (1999) Candidacidal activity prompted by N-terminus histatin-like domain of human salivary mucin (MUC7)1. Biochim Biophys Acta 1431:107-19
Tseng, C C; Miyamoto, M; Ramalingam, K et al. (1999) The roles of histidine residues at the starch-binding site in streptococcal-binding activities of human salivary amylase. Arch Oral Biol 44:119-27
Naganagowda, G A; Gururaja, T L; Satyanarayana, J et al. (1999) NMR analysis of human salivary mucin (MUC7) derived O-linked model glycopeptides: comparison of structural features and carbohydrate-peptide interactions. J Pept Res 54:290-310
Sojar, H T; Han, Y; Hamada, N et al. (1999) Role of the amino-terminal region of Porphyromonas gingivalis fimbriae in adherence to epithelial cells. Infect Immun 67:6173-6
Mettath, S; Munson, B R; Pandey, R K (1999) DNA interaction and photocleavage properties of porphyrins containing cationic substituents at the peripheral position. Bioconjug Chem 10:94-102
Naganagowda, G A; Gururaja, T L; Levine, M J (1998) Delineation of conformational preferences in human salivary statherin by 1H, 31P NMR and CD studies: sequential assignment and structure-function correlations. J Biomol Struct Dyn 16:91-107

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