High resolution structure analysis of Porphyromonas gingivalis membrane proteins in the biofilm.

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The purpose of this study is to identify and characterize new Porphyromonas gingivalis components that interact with Streptococcus oralis GAPDH. Pull-down assay was performed to detect potential interactions between P. gingivalis client proteins and S. oralis recombinant GAPDH. The proteins were separated by 2D-gel electrophoresis, and the five proteins ; RagA4, AbfD, GAPDH, GDH and MDH were identified by a proteomic-tandem mass spectrometry. Interaction between these P. gingivalis client proteins and S. oralis GAPDH was analyzed via a biomolecular interaction analysis system. S. oralis GAPDH demonstrated high affinity with five client proteins. Coaggregation between P. gingivalis and S. oralis was measured by turbidimetric method and fluorescence microscope. Recombinant RagA4, AbfD and GDH enhanced the coaggregation, whereas recombinant GAPDH and MDH inhibited in a dose-dependent manner. Furthermore, recombinant RagA4, AbfD and GDH regulated expression of luxS in P. gingivalis. These results indicate that five client membrane proteins of P. gingivalis might be regulators in P. gingivalis biofilm formation with oral streptococci.