Cargando…
Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis
Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics. Specifically, proteomics has helped determine and describe the physiological changes that lactic acid...
Autores principales: | , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8467624/ https://www.ncbi.nlm.nih.gov/pubmed/34577166 http://dx.doi.org/10.3390/molecules26185695 |
_version_ | 1784573445398331392 |
---|---|
author | Bagon, Bernadette B. Oh, Ju Kyoung Valeriano, Valerie Diane V. Pajarillo, Edward Alain B. Kang, Dae-Kyung |
author_facet | Bagon, Bernadette B. Oh, Ju Kyoung Valeriano, Valerie Diane V. Pajarillo, Edward Alain B. Kang, Dae-Kyung |
author_sort | Bagon, Bernadette B. |
collection | PubMed |
description | Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics. Specifically, proteomics has helped determine and describe the physiological changes that lactic acid bacteria undergo in specific conditions, especially in the host gut. In particular, the extracellular proteome, or exoproteome, of lactobacilli contains proteins specific to host– or environment–microbe interactions. Using gel-free, label-free ultra-high performance liquid chromatography tandem mass spectrometry, we explored the exoproteome of the probiotic candidate Lactobacillus mucosae LM1 subjected to bile treatment, to determine the proteins it may use against bile stress in the gut. Bile stress increased the size of the LM1 exoproteome, secreting ribosomal proteins (50S ribosomal protein L27 and L16) and metabolic proteins (lactate dehydrogenase, phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate dehydrogenases, among others) that might have moonlighting functions in the LM1 bile stress response. Interestingly, membrane-associated proteins (transporters, peptidase, ligase and cell division protein ftsH) were among the key proteins whose secretion were induced by the LM1 bile stress response. These specific proteins from LM1 exoproteome will be useful in observing the proposed bile response mechanisms via in vitro experiments. Our data also reveal the possible beneficial effects of LM1 to the host gut. |
format | Online Article Text |
id | pubmed-8467624 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-84676242021-09-27 Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis Bagon, Bernadette B. Oh, Ju Kyoung Valeriano, Valerie Diane V. Pajarillo, Edward Alain B. Kang, Dae-Kyung Molecules Article Lactobacillus sp. have long been studied for their great potential in probiotic applications. Recently, proteomics analysis has become a useful tool for studies on potential lactobacilli probiotics. Specifically, proteomics has helped determine and describe the physiological changes that lactic acid bacteria undergo in specific conditions, especially in the host gut. In particular, the extracellular proteome, or exoproteome, of lactobacilli contains proteins specific to host– or environment–microbe interactions. Using gel-free, label-free ultra-high performance liquid chromatography tandem mass spectrometry, we explored the exoproteome of the probiotic candidate Lactobacillus mucosae LM1 subjected to bile treatment, to determine the proteins it may use against bile stress in the gut. Bile stress increased the size of the LM1 exoproteome, secreting ribosomal proteins (50S ribosomal protein L27 and L16) and metabolic proteins (lactate dehydrogenase, phosphoglycerate kinase, glyceraldehyde-3-phosphate dehydrogenase and pyruvate dehydrogenases, among others) that might have moonlighting functions in the LM1 bile stress response. Interestingly, membrane-associated proteins (transporters, peptidase, ligase and cell division protein ftsH) were among the key proteins whose secretion were induced by the LM1 bile stress response. These specific proteins from LM1 exoproteome will be useful in observing the proposed bile response mechanisms via in vitro experiments. Our data also reveal the possible beneficial effects of LM1 to the host gut. MDPI 2021-09-20 /pmc/articles/PMC8467624/ /pubmed/34577166 http://dx.doi.org/10.3390/molecules26185695 Text en © 2021 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Bagon, Bernadette B. Oh, Ju Kyoung Valeriano, Valerie Diane V. Pajarillo, Edward Alain B. Kang, Dae-Kyung Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis |
title | Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis |
title_full | Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis |
title_fullStr | Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis |
title_full_unstemmed | Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis |
title_short | Exploring the Bile Stress Response of Lactobacillus mucosae LM1 through Exoproteome Analysis |
title_sort | exploring the bile stress response of lactobacillus mucosae lm1 through exoproteome analysis |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8467624/ https://www.ncbi.nlm.nih.gov/pubmed/34577166 http://dx.doi.org/10.3390/molecules26185695 |
work_keys_str_mv | AT bagonbernadetteb exploringthebilestressresponseoflactobacillusmucosaelm1throughexoproteomeanalysis AT ohjukyoung exploringthebilestressresponseoflactobacillusmucosaelm1throughexoproteomeanalysis AT valerianovaleriedianev exploringthebilestressresponseoflactobacillusmucosaelm1throughexoproteomeanalysis AT pajarilloedwardalainb exploringthebilestressresponseoflactobacillusmucosaelm1throughexoproteomeanalysis AT kangdaekyung exploringthebilestressresponseoflactobacillusmucosaelm1throughexoproteomeanalysis |