Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> 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. <i>Klebsiella pneumoniae...

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Autores principales:	Emanuela Roscetto, Rosa Bellavita, Rossella Paolillo, Francesco Merlino, Nicola Molfetta, Paolo Grieco, Elisabetta Buommino, Maria Rosaria Catania
Formato:	article
Lenguaje:	EN
Publicado:	MDPI AG 2021
Materias:	<i>Klebsiella pneumoniae</i> ESKAPE multidrug resistance carbapenemases healthcare-associated infections antimicrobial peptides Therapeutics. Pharmacology RM1-950
Acceso en línea:	https://doaj.org/article/1ad3760843114b6ebd6ac427c755dd40
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spelling	oai:doaj.org-article:1ad3760843114b6ebd6ac427c755dd402021-11-25T16:22:37ZAntimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates10.3390/antibiotics101113122079-6382https://doaj.org/article/1ad3760843114b6ebd6ac427c755dd402021-10-01T00:00:00Zhttps://www.mdpi.com/2079-6382/10/11/1312https://doaj.org/toc/2079-6382Over 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. <i>Klebsiella pneumoniae</i> 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 <i>K. pneumoniae</i> clinical isolates. According to the antibiotic susceptibility assay, all the <i>K. pneumoniae</i> strains were resistant to at least one other class of antibiotics, in addition to beta-lactams. Peptides <b>1B</b> and <b>C</b> showed activity on all test strains, but the lipidated analogue <b>C</b> expressed the greater antimicrobial properties, with MIC values ranging from 6.25 to 25 µM. Furthermore, the peptide <b>C</b> 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.Emanuela RoscettoRosa BellavitaRossella PaolilloFrancesco MerlinoNicola MolfettaPaolo GriecoElisabetta BuomminoMaria Rosaria CataniaMDPI AGarticle<i>Klebsiella pneumoniae</i>ESKAPEmultidrug resistancecarbapenemaseshealthcare-associated infectionsantimicrobial peptidesTherapeutics. PharmacologyRM1-950ENAntibiotics, Vol 10, Iss 1312, p 1312 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	<i>Klebsiella pneumoniae</i> ESKAPE multidrug resistance carbapenemases healthcare-associated infections antimicrobial peptides Therapeutics. Pharmacology RM1-950
spellingShingle	<i>Klebsiella pneumoniae</i> ESKAPE multidrug resistance carbapenemases healthcare-associated infections antimicrobial peptides Therapeutics. Pharmacology RM1-950 Emanuela Roscetto Rosa Bellavita Rossella Paolillo Francesco Merlino Nicola Molfetta Paolo Grieco Elisabetta Buommino Maria Rosaria Catania Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates
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. <i>Klebsiella pneumoniae</i> 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 <i>K. pneumoniae</i> clinical isolates. According to the antibiotic susceptibility assay, all the <i>K. pneumoniae</i> strains were resistant to at least one other class of antibiotics, in addition to beta-lactams. Peptides <b>1B</b> and <b>C</b> showed activity on all test strains, but the lipidated analogue <b>C</b> expressed the greater antimicrobial properties, with MIC values ranging from 6.25 to 25 µM. Furthermore, the peptide <b>C</b> 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.
format	article
author	Emanuela Roscetto Rosa Bellavita Rossella Paolillo Francesco Merlino Nicola Molfetta Paolo Grieco Elisabetta Buommino Maria Rosaria Catania
author_facet	Emanuela Roscetto Rosa Bellavita Rossella Paolillo Francesco Merlino Nicola Molfetta Paolo Grieco Elisabetta Buommino Maria Rosaria Catania
author_sort	Emanuela Roscetto
title	Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates
title_short	Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates
title_full	Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates
title_fullStr	Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates
title_full_unstemmed	Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates
title_sort	antimicrobial activity of a lipidated temporin l analogue against carbapenemase-producing <i>klebsiella pneumoniae</i> clinical isolates
publisher	MDPI AG
publishDate	2021
url	https://doaj.org/article/1ad3760843114b6ebd6ac427c755dd40
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Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical Isolates

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