Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum

Lactobacillus plantarum is a frequently encountered inhabitant of the human intestinal tract, and some strains are marketed as probiotics. Their ability to adhere to mannose residues is a potentially interesting characteristic with regard to proposed probiotic features such as colonization of the intestinal surface and competitive exclusion of pathogens. In this study, the variable capacity of 14 L. plantarum strains to agglutinate Saccharomyces cerevisiae in a mannose-specific manner was determined and subsequently correlated with an L. plantarum WCFS1-based genome-wide genotype database. This led to the identification of four candidate mannose adhesin-encoding genes. Two genes primarily predicted to code for sortase-dependent cell surface proteins displayed a complete gene-trait match. Their involvement in mannose adhesion was corroborated by the finding that a sortase (srtA) mutant of L. plantarum WCFS1 lost the capacity to agglutinate S. cerevisiae. The postulated role of these two candidate genes was investigated by gene-specific deletion and overexpression in L. plantarum WCFS1. Subsequent evaluation of the mannose adhesion capacity of the resulting mutant strains showed that inactivation of one candidate gene (lp_0373) did not affect mannose adhesion properties. In contrast, deletion of the other gene (lp_1229) resulted in a complete loss of yeast agglutination ability, while its overexpression quantitatively enhanced this phenotype. Therefore, this gene was designated to encode the mannose-specific adhesin (Msa; gene name, msa) of L. plantarum. Domain homology analysis of the predicted 1,000-residue Msa protein identified known carbohydrate-binding domains, further supporting its role as a mannose adhesin that is likely to be involved in the interaction of L. plantarum with its host in the intestinal tract

Saved in:
Bibliographic Details
Main Authors: Pretzer, G., Snel, J., Molenaar, D., Wiersma, A., Bron, P.A., Lambert, J.M., de Vos, W.M., van der Meer, R., Smits, M.A., Kleerebezem, M.
Format: Article/Letter to editor biblioteca
Language:English
Subjects:crystal-structure, epithelial-cells, escherichia-coli, human gastrointestinal-tract, lactic-acid bacteria, lactococcus-lactis, nucleotide-sequence, pseudomonas-aeruginosa, staphylococcus-aureus, surface-proteins,
Online Access:https://research.wur.nl/en/publications/biodiversity-based-identification-and-functional-characterization
Tags: Add Tag
No Tags, Be the first to tag this record!
id dig-wur-nl-wurpubs-340754
record_format koha
spelling dig-wur-nl-wurpubs-3407542025-01-23 Pretzer, G. Snel, J. Molenaar, D. Wiersma, A. Bron, P.A. Lambert, J.M. de Vos, W.M. van der Meer, R. Smits, M.A. Kleerebezem, M. Article/Letter to editor Journal of Bacteriology 187 (2005) 17 ISSN: 0021-9193 Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum 2005 Lactobacillus plantarum is a frequently encountered inhabitant of the human intestinal tract, and some strains are marketed as probiotics. Their ability to adhere to mannose residues is a potentially interesting characteristic with regard to proposed probiotic features such as colonization of the intestinal surface and competitive exclusion of pathogens. In this study, the variable capacity of 14 L. plantarum strains to agglutinate Saccharomyces cerevisiae in a mannose-specific manner was determined and subsequently correlated with an L. plantarum WCFS1-based genome-wide genotype database. This led to the identification of four candidate mannose adhesin-encoding genes. Two genes primarily predicted to code for sortase-dependent cell surface proteins displayed a complete gene-trait match. Their involvement in mannose adhesion was corroborated by the finding that a sortase (srtA) mutant of L. plantarum WCFS1 lost the capacity to agglutinate S. cerevisiae. The postulated role of these two candidate genes was investigated by gene-specific deletion and overexpression in L. plantarum WCFS1. Subsequent evaluation of the mannose adhesion capacity of the resulting mutant strains showed that inactivation of one candidate gene (lp_0373) did not affect mannose adhesion properties. In contrast, deletion of the other gene (lp_1229) resulted in a complete loss of yeast agglutination ability, while its overexpression quantitatively enhanced this phenotype. Therefore, this gene was designated to encode the mannose-specific adhesin (Msa; gene name, msa) of L. plantarum. Domain homology analysis of the predicted 1,000-residue Msa protein identified known carbohydrate-binding domains, further supporting its role as a mannose adhesin that is likely to be involved in the interaction of L. plantarum with its host in the intestinal tract en application/pdf https://research.wur.nl/en/publications/biodiversity-based-identification-and-functional-characterization 10.1128/JB.187.17.6128-6136.2005 https://edepot.wur.nl/20832 crystal-structure epithelial-cells escherichia-coli human gastrointestinal-tract lactic-acid bacteria lactococcus-lactis nucleotide-sequence pseudomonas-aeruginosa staphylococcus-aureus surface-proteins Wageningen University & Research
institution WUR NL
collection DSpace
country Países bajos
countrycode NL
component Bibliográfico
access En linea
databasecode dig-wur-nl
tag biblioteca
region Europa del Oeste
libraryname WUR Library Netherlands
language English
topic crystal-structure
epithelial-cells
escherichia-coli
human gastrointestinal-tract
lactic-acid bacteria
lactococcus-lactis
nucleotide-sequence
pseudomonas-aeruginosa
staphylococcus-aureus
surface-proteins
crystal-structure
epithelial-cells
escherichia-coli
human gastrointestinal-tract
lactic-acid bacteria
lactococcus-lactis
nucleotide-sequence
pseudomonas-aeruginosa
staphylococcus-aureus
surface-proteins
spellingShingle crystal-structure
epithelial-cells
escherichia-coli
human gastrointestinal-tract
lactic-acid bacteria
lactococcus-lactis
nucleotide-sequence
pseudomonas-aeruginosa
staphylococcus-aureus
surface-proteins
crystal-structure
epithelial-cells
escherichia-coli
human gastrointestinal-tract
lactic-acid bacteria
lactococcus-lactis
nucleotide-sequence
pseudomonas-aeruginosa
staphylococcus-aureus
surface-proteins
Pretzer, G.
Snel, J.
Molenaar, D.
Wiersma, A.
Bron, P.A.
Lambert, J.M.
de Vos, W.M.
van der Meer, R.
Smits, M.A.
Kleerebezem, M.
Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
description Lactobacillus plantarum is a frequently encountered inhabitant of the human intestinal tract, and some strains are marketed as probiotics. Their ability to adhere to mannose residues is a potentially interesting characteristic with regard to proposed probiotic features such as colonization of the intestinal surface and competitive exclusion of pathogens. In this study, the variable capacity of 14 L. plantarum strains to agglutinate Saccharomyces cerevisiae in a mannose-specific manner was determined and subsequently correlated with an L. plantarum WCFS1-based genome-wide genotype database. This led to the identification of four candidate mannose adhesin-encoding genes. Two genes primarily predicted to code for sortase-dependent cell surface proteins displayed a complete gene-trait match. Their involvement in mannose adhesion was corroborated by the finding that a sortase (srtA) mutant of L. plantarum WCFS1 lost the capacity to agglutinate S. cerevisiae. The postulated role of these two candidate genes was investigated by gene-specific deletion and overexpression in L. plantarum WCFS1. Subsequent evaluation of the mannose adhesion capacity of the resulting mutant strains showed that inactivation of one candidate gene (lp_0373) did not affect mannose adhesion properties. In contrast, deletion of the other gene (lp_1229) resulted in a complete loss of yeast agglutination ability, while its overexpression quantitatively enhanced this phenotype. Therefore, this gene was designated to encode the mannose-specific adhesin (Msa; gene name, msa) of L. plantarum. Domain homology analysis of the predicted 1,000-residue Msa protein identified known carbohydrate-binding domains, further supporting its role as a mannose adhesin that is likely to be involved in the interaction of L. plantarum with its host in the intestinal tract
format Article/Letter to editor
topic_facet crystal-structure
epithelial-cells
escherichia-coli
human gastrointestinal-tract
lactic-acid bacteria
lactococcus-lactis
nucleotide-sequence
pseudomonas-aeruginosa
staphylococcus-aureus
surface-proteins
author Pretzer, G.
Snel, J.
Molenaar, D.
Wiersma, A.
Bron, P.A.
Lambert, J.M.
de Vos, W.M.
van der Meer, R.
Smits, M.A.
Kleerebezem, M.
author_facet Pretzer, G.
Snel, J.
Molenaar, D.
Wiersma, A.
Bron, P.A.
Lambert, J.M.
de Vos, W.M.
van der Meer, R.
Smits, M.A.
Kleerebezem, M.
author_sort Pretzer, G.
title Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
title_short Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
title_full Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
title_fullStr Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
title_full_unstemmed Biodiversity-based identification and functional characterization of the mannose-specific adhesin of Lactobacillus plantarum
title_sort biodiversity-based identification and functional characterization of the mannose-specific adhesin of lactobacillus plantarum
url https://research.wur.nl/en/publications/biodiversity-based-identification-and-functional-characterization
work_keys_str_mv AT pretzerg biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT snelj biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT molenaard biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT wiersmaa biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT bronpa biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT lambertjm biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT devoswm biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT vandermeerr biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT smitsma biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
AT kleerebezemm biodiversitybasedidentificationandfunctionalcharacterizationofthemannosespecificadhesinoflactobacillusplantarum
_version_ 1822274494087036928