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Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain
Penicillin-binding proteins (PBPs) are responsible for peptidoglycan synthesis. By using biotinylated ampicillin, we detected PBPs of Lactobacillus paracasei strains. Ten PBPs were identified, 7 of which had apparent molecular sizes similar to those of Escherichia coli. In the presence of cholate, s...
Autores principales: | , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
BMFH Press
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5395426/ https://www.ncbi.nlm.nih.gov/pubmed/28439489 http://dx.doi.org/10.12938/bmfh.16-019 |
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author | HATTORI, Masahiro TORRES, Glaezel Angelique TANAKA, Naoto OKADA, Sanae ENDO, Akihito NAKAGAWA, Junichi |
author_facet | HATTORI, Masahiro TORRES, Glaezel Angelique TANAKA, Naoto OKADA, Sanae ENDO, Akihito NAKAGAWA, Junichi |
author_sort | HATTORI, Masahiro |
collection | PubMed |
description | Penicillin-binding proteins (PBPs) are responsible for peptidoglycan synthesis. By using biotinylated ampicillin, we detected PBPs of Lactobacillus paracasei strains. Ten PBPs were identified, 7 of which had apparent molecular sizes similar to those of Escherichia coli. In the presence of cholate, strain NRIC 0625 showed an elongated shape, and its putative PBP3 showed cholate-sensitive penicillin-binding activity. Furthermore, this strain was highly sensitive to cefalexin, which is known to inhibit cell division by inactivating PBP3. These results suggest that the septum synthetase PBP3 of lactic acid bacteria can be one of the targets of intestinal bile acid. |
format | Online Article Text |
id | pubmed-5395426 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | BMFH Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-53954262017-04-24 Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain HATTORI, Masahiro TORRES, Glaezel Angelique TANAKA, Naoto OKADA, Sanae ENDO, Akihito NAKAGAWA, Junichi Biosci Microbiota Food Health Note Penicillin-binding proteins (PBPs) are responsible for peptidoglycan synthesis. By using biotinylated ampicillin, we detected PBPs of Lactobacillus paracasei strains. Ten PBPs were identified, 7 of which had apparent molecular sizes similar to those of Escherichia coli. In the presence of cholate, strain NRIC 0625 showed an elongated shape, and its putative PBP3 showed cholate-sensitive penicillin-binding activity. Furthermore, this strain was highly sensitive to cefalexin, which is known to inhibit cell division by inactivating PBP3. These results suggest that the septum synthetase PBP3 of lactic acid bacteria can be one of the targets of intestinal bile acid. BMFH Press 2016-11-25 2017 /pmc/articles/PMC5395426/ /pubmed/28439489 http://dx.doi.org/10.12938/bmfh.16-019 Text en BMFH Press This is an open-access article distributed under the terms of the Creative Commons Attribution Non-Commercial No Derivatives (by-nc-nd) License. (CC-BY-NC-ND 4.0: https://creativecommons.org/licenses/by-nc-nd/4.0/) |
spellingShingle | Note HATTORI, Masahiro TORRES, Glaezel Angelique TANAKA, Naoto OKADA, Sanae ENDO, Akihito NAKAGAWA, Junichi Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
title | Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
title_full | Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
title_fullStr | Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
title_full_unstemmed | Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
title_short | Detection and analysis of Lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
title_sort | detection and analysis of lactobacillus paracasei penicillin-binding proteins revealed the presence of cholate-sensitive penicillin-binding protein 3 and an elongated cell shape in a cholate-sensitive strain |
topic | Note |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5395426/ https://www.ncbi.nlm.nih.gov/pubmed/28439489 http://dx.doi.org/10.12938/bmfh.16-019 |
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