Effect of histatin-5 and lysozyme on the ability of Streptococcus mutans to form biofilms in in vitro conditions

Postepy Hig Med Dosw (Online). 2015 Sep 20:69:1056-66.

Abstract

Introduction: The mechanisms of adhesion to solid surfaces enable S. mutans to colonize oral cavities and form biofilms, which play an important role in caries development. Additional properties enabling the survival of S. mutans in the oral cavity include its ability to survive in acidic environments and specific interactions with other microorganisms inhabiting this ecosystem.

Aim of the study: The aim of this study was to determine the antibacterial activity of saliva histatin-5 (peptide) and lysozyme (protein) against S. mutans and L. rhamnosus, as representatives of physiological flora.

Materials and methods: The study involved strains of physiological (L. rhamnosus) and cariogenic (S. mutans) flora isolated from one patient with diagnosed early caries of the deciduous teeth.

Results: It was proved that the presence of probiotic L. rhamnosus bacteria in the environment had a negative impact on the ability of S. mutans to produce biofilm. Moreover, the antibacterial activity of histatin-5 was confirmed, and it inhibited S. mutans growth at concentrations of 27.2 μg/ml and 54.4 μg/ml, both individually and in a mixture with lysozyme (in a total concentration of 54.4 μg/ml).

Conclusions: The data obtained constitute a promising result due to their potential future application in the prevention and early diagnosis of caries.

Publication types

  • Review

MeSH terms

  • Biofilms / drug effects*
  • Biofilms / growth & development*
  • Cell Adhesion / drug effects
  • Dental Caries / microbiology
  • Histatins / pharmacology*
  • Humans
  • Lacticaseibacillus rhamnosus / drug effects
  • Lacticaseibacillus rhamnosus / growth & development*
  • Mouth / microbiology
  • Muramidase / pharmacology*
  • Saliva / microbiology
  • Streptococcus mutans / drug effects
  • Streptococcus mutans / growth & development*

Substances

  • Histatins
  • Muramidase