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Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates

Over the years, the increasing acquisition of antibiotic resistance genes has led to the emergence of highly resistant bacterial strains and the loss of standard antibiotics’ efficacy, including β-lactam/β-lactamase inhibitor combinations and the last line carbapenems. Klebsiella pneumoniae is consi...

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Autores principales: Roscetto, Emanuela, Bellavita, Rosa, Paolillo, Rossella, Merlino, Francesco, Molfetta, Nicola, Grieco, Paolo, Buommino, Elisabetta, Catania, Maria Rosaria
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8614721/
https://www.ncbi.nlm.nih.gov/pubmed/34827250
http://dx.doi.org/10.3390/antibiotics10111312
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author Roscetto, Emanuela
Bellavita, Rosa
Paolillo, Rossella
Merlino, Francesco
Molfetta, Nicola
Grieco, Paolo
Buommino, Elisabetta
Catania, Maria Rosaria
author_facet Roscetto, Emanuela
Bellavita, Rosa
Paolillo, Rossella
Merlino, Francesco
Molfetta, Nicola
Grieco, Paolo
Buommino, Elisabetta
Catania, Maria Rosaria
author_sort Roscetto, Emanuela
collection PubMed
description Over the years, the increasing acquisition of antibiotic resistance genes has led to the emergence of highly resistant bacterial strains and the loss of standard antibiotics’ efficacy, including β-lactam/β-lactamase inhibitor combinations and the last line carbapenems. Klebsiella pneumoniae is considered one of the major exponents of a group of multidrug-resistant ESKAPE pathogens responsible for serious healthcare-associated infections. In this study, we proved the antimicrobial activity of two analogues of Temporin L against twenty carbapenemase-producing K. pneumoniae clinical isolates. According to the antibiotic susceptibility assay, all the K. pneumoniae strains were resistant to at least one other class of antibiotics, in addition to beta-lactams. Peptides 1B and C showed activity on all test strains, but the lipidated analogue C expressed the greater antimicrobial properties, with MIC values ranging from 6.25 to 25 µM. Furthermore, the peptide C showed bactericidal activity at MIC values. The results clearly highlight the great potential of antimicrobial peptides both as a new treatment option for difficult-to-treat infections and as a new strategy of drug-resistance control.
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spelling pubmed-86147212021-11-26 Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates Roscetto, Emanuela Bellavita, Rosa Paolillo, Rossella Merlino, Francesco Molfetta, Nicola Grieco, Paolo Buommino, Elisabetta Catania, Maria Rosaria Antibiotics (Basel) Article Over the years, the increasing acquisition of antibiotic resistance genes has led to the emergence of highly resistant bacterial strains and the loss of standard antibiotics’ efficacy, including β-lactam/β-lactamase inhibitor combinations and the last line carbapenems. Klebsiella pneumoniae is considered one of the major exponents of a group of multidrug-resistant ESKAPE pathogens responsible for serious healthcare-associated infections. In this study, we proved the antimicrobial activity of two analogues of Temporin L against twenty carbapenemase-producing K. pneumoniae clinical isolates. According to the antibiotic susceptibility assay, all the K. pneumoniae strains were resistant to at least one other class of antibiotics, in addition to beta-lactams. Peptides 1B and C showed activity on all test strains, but the lipidated analogue C expressed the greater antimicrobial properties, with MIC values ranging from 6.25 to 25 µM. Furthermore, the peptide C showed bactericidal activity at MIC values. The results clearly highlight the great potential of antimicrobial peptides both as a new treatment option for difficult-to-treat infections and as a new strategy of drug-resistance control. MDPI 2021-10-28 /pmc/articles/PMC8614721/ /pubmed/34827250 http://dx.doi.org/10.3390/antibiotics10111312 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
Roscetto, Emanuela
Bellavita, Rosa
Paolillo, Rossella
Merlino, Francesco
Molfetta, Nicola
Grieco, Paolo
Buommino, Elisabetta
Catania, Maria Rosaria
Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates
title Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates
title_full Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates
title_fullStr Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates
title_full_unstemmed Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates
title_short Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing Klebsiella pneumoniae Clinical Isolates
title_sort antimicrobial activity of a lipidated temporin l analogue against carbapenemase-producing klebsiella pneumoniae clinical isolates
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8614721/
https://www.ncbi.nlm.nih.gov/pubmed/34827250
http://dx.doi.org/10.3390/antibiotics10111312
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