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Research Article

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Functional Analysis of the p40 and p75 Proteins from Lactobacillus casei BL23

Bäuerl C.a · Pérez-Martínez G.a · Yan F.b · Polk D.B.c · Monedero V.a

Author affiliations

aLaboratorio de Bacterias Lácticas y Probióticos, Instituto de Agroquímica y Tecnología de Alimentos (CSIC), Burjassot, Valencia, Spain; bDepartment of Pediatrics, Division of Gastroenterology, Hepatology and Nutrition, Vanderbilt University School of Medicine and the Monroe Carell Jr. Children’s Hospital at Vanderbilt, Nashville, Tenn., and cDepartment of Pediatrics, University of Southern California and Children’s Hospital Los Angeles, Los Angeles, Calif., USA

Corresponding Author

Vicente Monedero

Laboratorio de Bacterias Lácticas y Probióticos

Instituto de Agroquímica y Tecnología de Alimentos (CSIC)

PO Box 73, ES–46100 Burjassot, Valencia (Spain)

Tel. +34 963 900 022, Fax +34 963 636 301, E-Mail btcmon@iata.csic.es

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The genomes of Lactobacillus casei/paracasei and Lactobacillus rhamnosus strains carry two genes encoding homologues of p40 and p75 from L. rhamnosus GG, two secreted proteins which display anti-apoptotic and cell protective effects on human intestinal epithelial cells. p40 and p75 carry cysteine, histidine-dependent aminohydrolase/peptidase (CHAP) and NLPC/P60 domains, respectively, which are characteristic of proteins with cell-wall hydrolase activity. In L. casei BL23 both proteins were secreted to the growth medium and were also located at the bacterial cell surface. The genes coding for both proteins were inactivated in this strain. Inactivation of LCABL_00230 (encoding p40) did not result in a significant difference in phenotype, whereas a mutation in LCABL_02770 (encoding p75) produced cells that formed very long chains. Purified glutathione-S-transferase (GST)-p40 and -p75 fusion proteins were able to hydrolyze the muropeptides from L. casei cell walls. Both fusions bound to mucin, collagen and to intestinal epithelial cells and, similar to L. rhamnosus GG p40, stimulated epidermal growth factor receptor phosphorylation in mouse intestine ex vivo. These results indicate that extracellular proteins belonging to the machinery of cell-wall metabolism in the closely related L. casei/paracasei-L. rhamnosus group are most likely involved in the probiotic effects described for these bacteria

© 2010 S. Karger AG, Basel

Article / Publication Details

First-Page Preview
Abstract of Research Article

Published online: December 17, 2010
Issue release date: January 2011

Number of Print Pages: 11
Number of Figures: 8
Number of Tables: 1

ISSN: 1464-1801 (Print)
eISSN: 1660-2412 (Online)

For additional information: http://www.karger.com/MMB

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