The primary goal of the RCOB at State University of New York at Buffalo is to expand the scientific base that underlies the nation's capability to prevent and control oral diseases and disorders and to improve oral health. Our scientific expertise and facilities were greatly expanded during the previous granting period through a combination of RCOB and University resources. This enables RCOB scientists to address scientific problems in an integrated fashion using protein chemistry, molecular biology, biophysics, immunology, microbiology and cell biology. The secondary goal of the RCOB is to maintain a center of excellence that will attract investigators of high quality to dental research, continue our long- standing tradition of research training at all levels of career development, and serve as a focal point to encourage productive research- related collaborations with other institutions. The Center uses the combined efforts of a team of dentist-scientists, microbiologists, biochemists, biophysicists, molecular biologists and cell biologists from both the School of Dental Medicine and the School of Medicine and Biomedical Sciences at the University at Buffalo. Additionally, scientists from Roswell Park Cancer Institute and the University of Minnesota have joined the Center to augment research efforts. Projects 1, 2 and 3 propose to enhance the protective qualities of saliva by the design and development of salivary substitutes to combat plaque mediated disease in subjects with normal salivary flow as well as those with xerostomia. A multidisciplinary approach involving protein chemistry, molecular biology, biophysics and bioengineering will design and synthesize salivary substances with enhanced functions relating to bacterial clearance/adherence mechanisms and lubrication. Projects 4, 5 and 8 are designed to characterize virulence factors of Porphyromonas gingivalis that might be determinants of disease and to study the immunochemical, biochemical and molecular biological mechanisms by which these factors are expressed and subsequently modulated. Studies will focus on the role of fimbriae in adhesion and outer membrane proteins in bacterial coaggregation and iron regulation.

Agency
National Institute of Health (NIH)
Institute
National Institute of Dental & Craniofacial Research (NIDCR)
Type
Specialized Center (P50)
Project #
5P50DE008240-09
Application #
2130024
Study Section
Special Emphasis Panel (SRC (10))
Project Start
1987-09-01
Project End
1997-08-31
Budget Start
1995-09-01
Budget End
1996-08-31
Support Year
9
Fiscal Year
1995
Total Cost
Indirect Cost
Name
State University of New York at Buffalo
Department
Dentistry
Type
Schools of Dentistry
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
Satyanarayana, J; Gururaja, T L; Naganagowda, G A et al. (1998) A concise methodology for the stereoselective synthesis of O-glycosylated amino acid building blocks: complete 1H NMR assignments and their application in solid-phase glycopeptide synthesis. J Pept Res 52:165-79

Showing the most recent 10 out of 162 publications