Characterization of binding of Streptococcus oralis glyceraldehyde-3-phosphate dehydrogenase to Porphyromonas gingivalis major fimbriae

Infect Immun. 2004 Sep;72(9):5475-7. doi: 10.1128/IAI.72.9.5475-5477.2004.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Biosensing Techniques
  • Fimbriae Proteins / genetics
  • Fimbriae Proteins / metabolism
  • Fimbriae, Bacterial / metabolism*
  • Glyceraldehyde-3-Phosphate Dehydrogenases / genetics
  • Glyceraldehyde-3-Phosphate Dehydrogenases / metabolism*
  • Humans
  • Kinetics
  • Porphyromonas gingivalis / metabolism*
  • Streptococcus oralis / enzymology*
  • Streptococcus oralis / metabolism

Substances

  • fimbrillin
  • Fimbriae Proteins
  • Glyceraldehyde-3-Phosphate Dehydrogenases