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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| Format: | Article |
| Language: | English |
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MDPI AG
2021-10-01
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| Series: | Antibiotics |
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| Online Access: | https://www.mdpi.com/2079-6382/10/11/1312 |
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| 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 |
| collection | DOAJ |
| 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. |
| first_indexed | 2024-03-10T05:45:50Z |
| format | Article |
| id | doaj.art-1ad3760843114b6ebd6ac427c755dd40 |
| institution | Directory Open Access Journal |
| issn | 2079-6382 |
| language | English |
| last_indexed | 2024-03-10T05:45:50Z |
| publishDate | 2021-10-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antibiotics |
| spelling | doaj.art-1ad3760843114b6ebd6ac427c755dd402023-11-22T22:09:45ZengMDPI AGAntibiotics2079-63822021-10-011011131210.3390/antibiotics10111312Antimicrobial Activity of a Lipidated Temporin L Analogue against Carbapenemase-Producing <i>Klebsiella pneumoniae</i> Clinical IsolatesEmanuela Roscetto0Rosa Bellavita1Rossella Paolillo2Francesco Merlino3Nicola Molfetta4Paolo Grieco5Elisabetta Buommino6Maria Rosaria Catania7Department of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Via S. Pansini 5, 80131 Naples, ItalyDepartment of Pharmacy, University of Naples Federico II, Via Montesano 49, 80131 Naples, ItalyDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Via S. Pansini 5, 80131 Naples, ItalyDepartment of Pharmacy, University of Naples Federico II, Via Montesano 49, 80131 Naples, ItalyDepartment of Pharmacy, University of Naples Federico II, Via Montesano 49, 80131 Naples, ItalyDepartment of Pharmacy, University of Naples Federico II, Via Montesano 49, 80131 Naples, ItalyDepartment of Pharmacy, University of Naples Federico II, Via Montesano 49, 80131 Naples, ItalyDepartment of Molecular Medicine and Medical Biotechnology, University of Naples Federico II, Via S. Pansini 5, 80131 Naples, ItalyOver 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.https://www.mdpi.com/2079-6382/10/11/1312<i>Klebsiella pneumoniae</i>ESKAPEmultidrug resistancecarbapenemaseshealthcare-associated infectionsantimicrobial peptides |
| spellingShingle | 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 Antibiotics <i>Klebsiella pneumoniae</i> ESKAPE multidrug resistance carbapenemases healthcare-associated infections antimicrobial peptides |
| title | 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_short | 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 |
| topic | <i>Klebsiella pneumoniae</i> ESKAPE multidrug resistance carbapenemases healthcare-associated infections antimicrobial peptides |
| url | https://www.mdpi.com/2079-6382/10/11/1312 |
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