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

Borja Sánchez1, María C Urdaci

  • 1Instituto de Productos Lácteos de Asturias, Consejo Superior de Investigaciones Científicas, Ctra. Infiesto s/n, 33300 Villaviciosa, Asturias, Spain. borja@ipla.csic.es

Current Microbiology
|March 31, 2012
PubMed

Insights

Extracellular proteins from Lactobacillus plantarum BMCM12 significantly inhibit gut pathogen adhesion to mucin. These findings highlight the potential of these proteins in preventing pathogen colonization in the gut.

Area of Science:

  • Microbiology
  • Proteomics
  • Gastroenterology

Background:

  • Gut pathogens can adhere to the intestinal lining, leading to infections.
  • Lactobacillus plantarum is a probiotic bacterium with potential health benefits.
  • Extracellular proteins secreted by probiotics may play a role in modulating the gut environment.

Purpose of the Study:

  • To investigate the anti-adhesion properties of extracellular proteins from Lactobacillus plantarum BMCM12 against gut pathogens.
  • To identify and characterize these extracellular proteins.

Main Methods:

  • Precipitation and SDS-PAGE of extracellular proteins from L. plantarum BMCM12.
  • Tandem mass spectrometry for protein identification.
  • Glycoprotein staining and de-glycosylation assays.
  • In vitro assays to assess pathogen adhesion to mucin (using Escherichia coli and Salmonella enterica).

Main Results:

  • Extracellular proteins from L. plantarum BMCM12 were identified, with evidence of glycosylation.
  • These proteins significantly reduced the adhesion of Escherichia coli and Salmonella enterica to mucin.
  • The inhibitory effect was observed when proteins were added prior to pathogen exposure.

Conclusions:

  • Extracellular proteins from L. plantarum BMCM12 possess anti-adhesion properties against common gut pathogens.
  • These proteins are potential candidates for developing strategies to prevent pathogen colonization in the gut.
  • Protein glycosylation may contribute to the functional activity of these extracellular proteins.

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