Cargando…
Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin
Clostridioides difficile is the leading cause of antibiotic-associated diarrhea but can also result in more serious, life-threatening conditions. The incidence of C. difficile infections in hospitals is increasing, both in frequency and severity, and antibiotic-resistant C. difficile strains are adv...
Autores principales: | , , , , , , , |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2021
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7918085/ https://www.ncbi.nlm.nih.gov/pubmed/33670309 http://dx.doi.org/10.3390/cells10020372 |
_version_ | 1783657847567941632 |
---|---|
author | Maaß, Sandra Bartel, Jürgen Mücke, Pierre-Alexander Schlüter, Rabea Sura, Thomas Zaschke-Kriesche, Julia Smits, Sander H. J. Becher, Dörte |
author_facet | Maaß, Sandra Bartel, Jürgen Mücke, Pierre-Alexander Schlüter, Rabea Sura, Thomas Zaschke-Kriesche, Julia Smits, Sander H. J. Becher, Dörte |
author_sort | Maaß, Sandra |
collection | PubMed |
description | Clostridioides difficile is the leading cause of antibiotic-associated diarrhea but can also result in more serious, life-threatening conditions. The incidence of C. difficile infections in hospitals is increasing, both in frequency and severity, and antibiotic-resistant C. difficile strains are advancing. Against this background antimicrobial peptides (AMPs) are an interesting alternative to classic antibiotics. Information on the effects of AMPs on C. difficile will not only enhance the knowledge for possible biomedical application but may also provide insights into mechanisms of C. difficile to adapt or counteract AMPs. This study applies state-of-the-art mass spectrometry methods to quantitatively investigate the proteomic response of C. difficile 630∆erm to sublethal concentrations of the AMP nisin allowing to follow the cellular stress adaptation in a time-resolved manner. The results do not only point at a heavy reorganization of the cellular envelope but also resulted in pronounced changes in central cellular processes such as carbohydrate metabolism. Further, the number of flagella per cell was increased during the adaptation process. The potential involvement of flagella in nisin adaptation was supported by a more resistant phenotype exhibited by a non-motile but hyper-flagellated mutant. |
format | Online Article Text |
id | pubmed-7918085 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-79180852021-03-02 Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin Maaß, Sandra Bartel, Jürgen Mücke, Pierre-Alexander Schlüter, Rabea Sura, Thomas Zaschke-Kriesche, Julia Smits, Sander H. J. Becher, Dörte Cells Article Clostridioides difficile is the leading cause of antibiotic-associated diarrhea but can also result in more serious, life-threatening conditions. The incidence of C. difficile infections in hospitals is increasing, both in frequency and severity, and antibiotic-resistant C. difficile strains are advancing. Against this background antimicrobial peptides (AMPs) are an interesting alternative to classic antibiotics. Information on the effects of AMPs on C. difficile will not only enhance the knowledge for possible biomedical application but may also provide insights into mechanisms of C. difficile to adapt or counteract AMPs. This study applies state-of-the-art mass spectrometry methods to quantitatively investigate the proteomic response of C. difficile 630∆erm to sublethal concentrations of the AMP nisin allowing to follow the cellular stress adaptation in a time-resolved manner. The results do not only point at a heavy reorganization of the cellular envelope but also resulted in pronounced changes in central cellular processes such as carbohydrate metabolism. Further, the number of flagella per cell was increased during the adaptation process. The potential involvement of flagella in nisin adaptation was supported by a more resistant phenotype exhibited by a non-motile but hyper-flagellated mutant. MDPI 2021-02-11 /pmc/articles/PMC7918085/ /pubmed/33670309 http://dx.doi.org/10.3390/cells10020372 Text en © 2021 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 Maaß, Sandra Bartel, Jürgen Mücke, Pierre-Alexander Schlüter, Rabea Sura, Thomas Zaschke-Kriesche, Julia Smits, Sander H. J. Becher, Dörte Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin |
title | Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin |
title_full | Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin |
title_fullStr | Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin |
title_full_unstemmed | Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin |
title_short | Proteomic Adaptation of Clostridioides difficile to Treatment with the Antimicrobial Peptide Nisin |
title_sort | proteomic adaptation of clostridioides difficile to treatment with the antimicrobial peptide nisin |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7918085/ https://www.ncbi.nlm.nih.gov/pubmed/33670309 http://dx.doi.org/10.3390/cells10020372 |
work_keys_str_mv | AT maaßsandra proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT barteljurgen proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT muckepierrealexander proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT schluterrabea proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT surathomas proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT zaschkekrieschejulia proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT smitssanderhj proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin AT becherdorte proteomicadaptationofclostridioidesdifficiletotreatmentwiththeantimicrobialpeptidenisin |