Identification of Surface Proteins from Lactobacillus casei BL23 Able to Bind Fibronectin and Collagen

Probiotics and Antimicrobial Proteins
Diego Muñoz-ProvencioVicente Monedero

Abstract

Strains of lactobacilli show the capacity to attach to extracellular matrix proteins. Cell-wall fractions of Lactobacillus casei BL23 enriched in fibronectin, and collagen-binding proteins were isolated. Mass spectrometry analysis of their protein content revealed the presence of stress-related proteins (GroEL, ClpL), translational elongation factors (EF-Tu, EF-G), oligopeptide solute-binding proteins, and the glycolytic enzymes enolase and glyceraldehyde-3-phosphate dehydrogenase (GAPDH). The latter two enzymes were expressed in Escherichia coli and purified as glutathione-S-transferase (GST) fusion proteins, and their in vitro binding activity to fibronectin and collagen was confirmed. These results reinforce the idea that lactobacilli display on their surfaces a variety of moonlighting proteins that can be important in their adaptation to survive at intestinal mucosal sites and in the interaction with host cells.

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Citations

Jul 24, 2014·Cellular Microbiology·Aurélie RieuJean Guzzo
Mar 24, 2017·FEMS Microbiology Letters·Ni Putu Desy AryantiniKenji Fukuda
Nov 22, 2016·Bioscience of Microbiota, Food and Health·Hideki KinoshitaTadao Saito
Sep 13, 2017·Scientific Reports·Michael WidjajaSteven Philip Djordjevic
Sep 2, 2020·Wellcome Open Research·Andrea LiaPietro Roversi

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