Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae.
Binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase (GAPDH) to Porphyromonas gingivalis fimbriae was characterized via a biomolecular interaction analysis system. The interaction was specific, and the association constant value was 4.34 x 10(7) M(-1), suggesting that S. oralis GAPDH functions as a dominant receptor for P. gingivalis and contributes to P. gingivalis colonization.
Department of Preventive Dentistry, Osaka University Graduate School of Dentistry, 1-8 Yamadaoka, Suita, Osaka 565-0871, Japan.
Kazuhiko
K
Maeda
Hideki
H
Nagata
Masae
M
Kuboniwa
Kosuke
K
Kataoka
Nobuko
N
Nishida
Muneo
M
Tanaka
Satoshi
S
Shizukuishi
D015374:Biosensing Techniques; D036781:Fimbriae Proteins / Q000235:genetics / Q000378:metabolism; D010861:Fimbriae, Bacterial / Q000378:metabolism*; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D007700:Kinetics; D016966:Porphyromonas gingivalis / Q000378:metabolism*; D019533:Streptococcus oralis / Q000201:enzymology* / Q000378:metabolism
C063055:fimbrillin; D036781:Fimbriae Proteins; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases