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The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics
Gram-negative bacteria have an outer membrane inhibiting the entry of antibiotics. Porins, found within the outer membrane, are involved in regulating the permeability of β-lactam antibiotics. β-lactamases are enzymes that are able to inactivate the antibacterial properties of β-lactam antibiotics....
Autores principales: | , , , , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215730/ https://www.ncbi.nlm.nih.gov/pubmed/32316670 http://dx.doi.org/10.3390/ijms21082822 |
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author | Kim, Si Won Lee, Jung Seok Park, Seong Bin Lee, Ae Rin Jung, Jae Wook Chun, Jin Hong Lazarte, Jassy Mary S. Kim, Jaesung Seo, Jong-Su Kim, Jong-Hwan Song, Jong-Wook Ha, Min Woo Thompson, Kim D. Lee, Chang-Ro Jung, Myunghwan Jung, Tae Sung |
author_facet | Kim, Si Won Lee, Jung Seok Park, Seong Bin Lee, Ae Rin Jung, Jae Wook Chun, Jin Hong Lazarte, Jassy Mary S. Kim, Jaesung Seo, Jong-Su Kim, Jong-Hwan Song, Jong-Wook Ha, Min Woo Thompson, Kim D. Lee, Chang-Ro Jung, Myunghwan Jung, Tae Sung |
author_sort | Kim, Si Won |
collection | PubMed |
description | Gram-negative bacteria have an outer membrane inhibiting the entry of antibiotics. Porins, found within the outer membrane, are involved in regulating the permeability of β-lactam antibiotics. β-lactamases are enzymes that are able to inactivate the antibacterial properties of β-lactam antibiotics. Interestingly, porins and β-lactamase are found in outer membrane vesicles (OMVs) of β-lactam-resistant Escherichia coli and may be involved in the survival of susceptible strains of E. coli in the presence of antibiotics, through the hydrolysis of the β-lactam antibiotic. In this study, OMVs isolated from β-lactam-resistant E. coli and from mutants, lacking porin or β-lactamase, were evaluated to establish if the porins or β-lactamase in OMVs were involved in the degradation of β-lactam antibiotics. OMVs isolated from E. coli deficient in β-lactamase did not show any degradation ability against β-lactam antibiotics, while OMVs lacking OmpC or OmpF showed significantly lower levels of hydrolyzing activity than OMVs from parent E. coli. These data reveal an important role of OMVs in bacterial defense mechanisms demonstrating that the OmpC and OmpF proteins allow permeation of β-lactam antibiotics into the lumen of OMVs, and antibiotics that enter the OMVs can be degraded by β-lactamase. |
format | Online Article Text |
id | pubmed-7215730 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-72157302020-05-22 The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics Kim, Si Won Lee, Jung Seok Park, Seong Bin Lee, Ae Rin Jung, Jae Wook Chun, Jin Hong Lazarte, Jassy Mary S. Kim, Jaesung Seo, Jong-Su Kim, Jong-Hwan Song, Jong-Wook Ha, Min Woo Thompson, Kim D. Lee, Chang-Ro Jung, Myunghwan Jung, Tae Sung Int J Mol Sci Article Gram-negative bacteria have an outer membrane inhibiting the entry of antibiotics. Porins, found within the outer membrane, are involved in regulating the permeability of β-lactam antibiotics. β-lactamases are enzymes that are able to inactivate the antibacterial properties of β-lactam antibiotics. Interestingly, porins and β-lactamase are found in outer membrane vesicles (OMVs) of β-lactam-resistant Escherichia coli and may be involved in the survival of susceptible strains of E. coli in the presence of antibiotics, through the hydrolysis of the β-lactam antibiotic. In this study, OMVs isolated from β-lactam-resistant E. coli and from mutants, lacking porin or β-lactamase, were evaluated to establish if the porins or β-lactamase in OMVs were involved in the degradation of β-lactam antibiotics. OMVs isolated from E. coli deficient in β-lactamase did not show any degradation ability against β-lactam antibiotics, while OMVs lacking OmpC or OmpF showed significantly lower levels of hydrolyzing activity than OMVs from parent E. coli. These data reveal an important role of OMVs in bacterial defense mechanisms demonstrating that the OmpC and OmpF proteins allow permeation of β-lactam antibiotics into the lumen of OMVs, and antibiotics that enter the OMVs can be degraded by β-lactamase. MDPI 2020-04-17 /pmc/articles/PMC7215730/ /pubmed/32316670 http://dx.doi.org/10.3390/ijms21082822 Text en © 2020 by the authors. 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 (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Kim, Si Won Lee, Jung Seok Park, Seong Bin Lee, Ae Rin Jung, Jae Wook Chun, Jin Hong Lazarte, Jassy Mary S. Kim, Jaesung Seo, Jong-Su Kim, Jong-Hwan Song, Jong-Wook Ha, Min Woo Thompson, Kim D. Lee, Chang-Ro Jung, Myunghwan Jung, Tae Sung The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics |
title | The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics |
title_full | The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics |
title_fullStr | The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics |
title_full_unstemmed | The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics |
title_short | The Importance of Porins and β-Lactamase in Outer Membrane Vesicles on the Hydrolysis of β-Lactam Antibiotics |
title_sort | importance of porins and β-lactamase in outer membrane vesicles on the hydrolysis of β-lactam antibiotics |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7215730/ https://www.ncbi.nlm.nih.gov/pubmed/32316670 http://dx.doi.org/10.3390/ijms21082822 |
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