A novel peptidic inhibitor derived from Streptococcus cristatus ArcA attenuates virulence potential of Porphyromonas gingivalis

Sci Rep. 2017 Nov 24;7(1):16217. doi: 10.1038/s41598-017-16522-y.

Abstract

Periodontitis is a global health problem and the 6th most common infectious disease worldwide. Porphyromonas gingivalis is considered a keystone pathogen in the disease and is capable of elevating the virulence potential of the periodontal microbial community. Strategies that interfere with P. gingivalis colonization and expression of virulence factor are therefore attractive approaches for preventing and treating periodontitis. We have previously reported that an 11-mer peptide (SAPP) derived from Streptococcus cristatus arginine deiminase (ArcA) was able to repress the expression and production of several well-known P. gingivalis virulence factors including fimbrial proteins and gingipains. Herein we expand and develop these studies to ascertain the impact of this peptide on phenotypic properties of P. gingivalis related to virulence potential. We found that growth rate was not altered by exposure of P. gingivalis to SAPP, while monospecies and heterotypic biofilm formation, and invasion of oral epithelial cells were inhibited. Additionally, SAPP was able to impinge the ability of P. gingivalis to dysregulate innate immunity by repressing gingipain-associated degradation of interleukin-8 (IL8). Hence, SAPP has characteristics that could be exploited for the manipulation of P. gingivalis levels in oral communities and preventing realization of virulence potential.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Bacterial Proteins / metabolism
  • Bacterial Proteins / pharmacology*
  • Biofilms / drug effects
  • Peptides / metabolism
  • Peptides / pharmacology*
  • Porphyromonas gingivalis / drug effects*
  • Porphyromonas gingivalis / pathogenicity
  • Streptococcus / metabolism*

Substances

  • Anti-Bacterial Agents
  • Bacterial Proteins
  • Peptides