Identification of Streptococcus cristatus peptides that repress expression of virulence genes in Porphyromonas gingivalis.
Meng-Hsuan HoRichard J LamontHua XiePublished in: Scientific reports (2017)
Dental plaque is a complex multispecies biofilm, and is a direct precursor of periodontal disease. The virulence of periodontal pathogens, such as Porphyromonas gingivalis, is expressed in the context of this polymicrobial community. Previously, we reported an antagonistic relationship between Streptococcus cristatus and P. gingivalis, and identified arginine deiminase (ArcA) of S. cristatus as the signaling molecule to which P. gingivalis responds by repressing the expression and production of FimA protein. Here we demonstrate that direct interaction between P. gingivalis and S. cristatus is necessary for the cell-cell communication. Two surface proteins of P. gingivalis, PGN_0294 and PGN_0806, were found to interact with S. cristatus ArcA. Using a peptide array analysis, we identified several P. gingivalis-binding sites of ArcA, which led to the discovery of an 11-mer peptide with the native sequence of ArcA that repressed expression of fimbriae and of gingipains. These data indicate that a functional motif of ArcA is sufficient to selectively alter virulence gene expression in P. gingivalis, and PGN_0294 and PGN_0806 may serve as receptors for ArcA. Our findings provide a molecular basis for future rational design of agents that interfere with the initiation and formation of a P. gingivalis-induced pathogenic community.
Keyphrases
- biofilm formation
- pseudomonas aeruginosa
- staphylococcus aureus
- gene expression
- poor prognosis
- escherichia coli
- healthcare
- antimicrobial resistance
- mental health
- candida albicans
- binding protein
- nitric oxide
- high throughput
- stem cells
- high resolution
- single cell
- dna methylation
- amino acid
- endothelial cells
- cell therapy
- machine learning
- gram negative
- mass spectrometry
- bioinformatics analysis
- big data
- protein protein
- stress induced