Extracellular proteins from Lactobacillus plantarum BMCM12 prevent adhesion of enteropathogens to mucin

Curr Microbiol. 2012 Jun;64(6):592-6. doi: 10.1007/s00284-012-0115-6. Epub 2012 Mar 30.

Abstract

The aim of this study was to study the interference of the extracellular proteins produced by Lactobacillus plantarum BMCM12 with the adhesion of some well-known gut pathogens. The extracellular proteins secreted by L. plantarum BMCM12 in MRS broth were precipitated, resolved by SDS-PAGE, and identified by tandem mass spectrometry. Discordances between the observed and the theoretical molecular masses of several proteins suggested the presence of protein glycosylation, corroborated with specific glycoprotein staining after protein de-glycosylation using trifluoromethanesulfonic acid. Experiments of exclusion, competition, or prevention of the pathogen adhesion to mucin were performed using BMCM12 extracellular proteins, using Escherichia coli LMG2092 and Salmonella enterica subsp. enterica LMG15860. Extracellular proteins from BMCM12 reduced significantly the adhesion of the pathogens when they were added prior to adhesion assays. These proteins play thus important roles in preventing pathogen adhesion to the mucin layer.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Antibiosis*
  • Bacterial Adhesion*
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / isolation & purification
  • Bacterial Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Escherichia coli / physiology*
  • Lactobacillus plantarum / metabolism
  • Lactobacillus plantarum / physiology*
  • Molecular Weight
  • Mucins / metabolism*
  • Salmonella enterica / physiology*
  • Tandem Mass Spectrometry

Substances

  • Bacterial Proteins
  • Mucins