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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...

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Autores principales: Maaß, Sandra, Bartel, Jürgen, Mücke, Pierre-Alexander, Schlüter, Rabea, Sura, Thomas, Zaschke-Kriesche, Julia, Smits, Sander H. J., Becher, Dörte
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
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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.
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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
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