2-DE and MS analysis of key proteins in the adhesion of Lactobacillus plantarum, a first step toward early selection of probiotics based on bacterial biomarkers
The identification of cell components involved in probiotic activities is a challenge in current probiotic research. In this work, a new approach based on proteomics as an analytical tool for the identification of characteristic protein profiles related to adhesion to mucin as a model probiotic prop...
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| Published in | Electrophoresis Vol. 30; no. 6; pp. 949 - 956 |
|---|---|
| Main Authors | , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
Weinheim
Wiley-VCH Verlag
01.03.2009
WILEY-VCH Verlag WILEY‐VCH Verlag |
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| Abstract | The identification of cell components involved in probiotic activities is a challenge in current probiotic research. In this work, a new approach based on proteomics as an analytical tool for the identification of characteristic protein profiles related to adhesion to mucin as a model probiotic property was used. Three Lactobacillus plantarum strains with different adhesion rates were used for proteomic analysis: L. plantarum WHE 92 (15.9%), L. plantarum 299 v (9.1%) and L. plantarum CECT 4185 (1.4%). Cell wall extracts were subjected to proteomic analysis of differential protein expression using 2-DE, tryptic digestion, chip-LC-QTOF mass analysis and protein identification using database search. Several proteins, previously reported to be involved in bacterial adhesion: elongation factor EF-Tu, GroEL chaperonin, molecular chaperone DnaK and glyceraldehyde-3-phosphate dehydrogenase were found to be overexpressed in the cell wall proteome of the highly adhesive strain L. plantarum WHE 92. The overexpression of two spots containing GroES co-chaperonin in the most adhesive strain also suggested the involvement of this protein in the adhesion process. The association of proteomic profiles and proteins with particular probiotic properties opens the way for the use of such profiles and proteins as bacterial biomarkers for the properties of bacteria but probably also for their potential health effects. |
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| AbstractList | Abstract
The identification of cell components involved in probiotic activities is a challenge in current probiotic research. In this work, a new approach based on proteomics as an analytical tool for the identification of characteristic protein profiles related to adhesion to mucin as a model probiotic property was used. Three
Lactobacillus plantarum
strains with different adhesion rates were used for proteomic analysis:
L. plantarum
WHE 92 (15.9%),
L. plantarum
299 v (9.1%) and
L. plantarum
CECT 4185 (1.4%). Cell wall extracts were subjected to proteomic analysis of differential protein expression using 2‐DE, tryptic digestion, chip‐LC‐QTOF mass analysis and protein identification using database search. Several proteins, previously reported to be involved in bacterial adhesion: elongation factor EF‐Tu, GroEL chaperonin, molecular chaperone DnaK and glyceraldehyde‐3‐phosphate dehydrogenase were found to be overexpressed in the cell wall proteome of the highly adhesive strain
L. plantarum
WHE 92. The overexpression of two spots containing GroES co‐chaperonin in the most adhesive strain also suggested the involvement of this protein in the adhesion process. The association of proteomic profiles and proteins with particular probiotic properties opens the way for the use of such profiles and proteins as bacterial biomarkers for the properties of bacteria but probably also for their potential health effects. The identification of cell components involved in probiotic activities is a challenge in current probiotic research. In this work, a new approach based on proteomics as an analytical tool for the identification of characteristic protein profiles related to adhesion to mucin as a model probiotic property was used. Three Lactobacillus plantarum strains with different adhesion rates were used for proteomic analysis: L. plantarum WHE 92 (15.9%), L. plantarum 299 v (9.1%) and L. plantarum CECT 4185 (1.4%). Cell wall extracts were subjected to proteomic analysis of differential protein expression using 2-DE, tryptic digestion, chip-LC-QTOF mass analysis and protein identification using database search. Several proteins, previously reported to be involved in bacterial adhesion: elongation factor EF-Tu, GroEL chaperonin, molecular chaperone DnaK and glyceraldehyde-3-phosphate dehydrogenase were found to be overexpressed in the cell wall proteome of the highly adhesive strain L. plantarum WHE 92. The overexpression of two spots containing GroES co-chaperonin in the most adhesive strain also suggested the involvement of this protein in the adhesion process. The association of proteomic profiles and proteins with particular probiotic properties opens the way for the use of such profiles and proteins as bacterial biomarkers for the properties of bacteria but probably also for their potential health effects. |
| Author | Izquierdo, Esther Horvatovich, Peter Aoude-Werner, Dalal Marchioni, Eric Sanz, Yolanda Ennahar, Saïd |
| Author_xml | – sequence: 1 fullname: Izquierdo, Esther – sequence: 2 fullname: Horvatovich, Peter – sequence: 3 fullname: Marchioni, Eric – sequence: 4 fullname: Aoude-Werner, Dalal – sequence: 5 fullname: Sanz, Yolanda – sequence: 6 fullname: Ennahar, Saïd |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/19309013$$D View this record in MEDLINE/PubMed |
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| SubjectTerms | Adhesion Analysis of Variance Animals Bacteria Bacterial Proteins - analysis Biomarkers Biomarkers - analysis Cell Adhesion Cell Wall Chaperonin 10 - analysis Electrophoresis, Gel, Two-Dimensional Lactobacillus plantarum Lactobacillus plantarum - chemistry Lactobacillus plantarum - metabolism Mass Spectrometry Mucins - metabolism Probiotics Probiotics - chemistry Proteomics Swine |
| Title | 2-DE and MS analysis of key proteins in the adhesion of Lactobacillus plantarum, a first step toward early selection of probiotics based on bacterial biomarkers |
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