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Detection and Prevalence of Active Drug Efflux Mechanism in Various Multidrug-Resistant Klebsiella pneumoniae Strains from Turkey
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The prevalence of active drug efflux pump and porin alterations was investigated in Turkish nosocomial strains of Klebsiella pneumoniae exhibiting a multidrug-resistant phenotype. MICs of various antibiotics, including quinolones, chloramphenicol, tetracycline, and β-lactams, for those strains were determined either with or without the efflux pump inhibitor phenylalanine arginine β-naphthylamide (PAβN). Thirty-nine percent of the strains exhibited a PAβN-modulated resistance for quinolones, chloramphenicol, and tetracycline. In these strains, a significant increase of chloramphenicol accumulation was gained in the presence of the efflux pump inhibitor PAβN or with the energy uncoupler carbonyl cyanide m -chlorophenylhydrazone. Moreover, high-level expression of the membrane fusion protein AcrA, which was immunodetected in most of those isolates, suggests that the AcrAB/TolC efflux machinery contributed to their antibiotic resistance. Studies of K. pneumoniae porins indicated that the majority of the strains, including extended-spectrum β-lactamase producers and efflux-positive ones, presented an alteration in their sorbitol-sensitive porin (OmpK35) expression. This is the first report showing the prominent role of active drug efflux in the antibiotic resistance of nosocomial K. pneumoniae strains from Turkey.
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“This alteration in the type of porin expressed correlated with a 4 – 8 fold decrease in susceptibility for a wide range of β-lactam antimicrobials (41,42).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [41]
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“The post-therapy isolates were found to exhibit a shift in porin expression from OmpK35 to OmpK36 (the latter possessing a smaller channel size).”
From Mechanisms of Antibiotic Resistance (2016) · cites this paper as [41]
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Sekar, P., Mamtora, D., Bhalekar, P., & Krishnan, P. (2022) · Journal of Pure and Applied Microbiology · doi:10.22207/jpam.16.3.48 · Cited by 9
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Metadata
- Authors
- Hasdemir, U. O., Chevalier, J., Nordmann, P., & Pagès, J.-M.
- Affiliations
- Aix-Marseille Université (FR)
- Bicêtre Hospital (FR)
- Enveloppe Bactérienne, Perméabilité et Antibiotiques, EA 2197, IFR48, Faculté de Médecine, Université de la Mediterranée, Marseille
- Venue
- Journal of Clinical Microbiology
- Publisher
- American Society for Microbiology
- Published
- 2004-06
- Volume
- 42
- Issue
- 6
- Pages
- 2701-2706
- ISSN
- 0095-1137 (ISSN-L)
- 1098-660X
- PMC
- PMC427859
- OpenAlex
- W2151288894
- Cited by
- 131
- References
- 30
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 5 · 2023: 7 · 2022: 3 · 2021: 7 · 2020: 8 · 2019: 6 · 2018: 7 · 2017: 7 · 2016: 16 · 2015: 2 · 2014: 9 · 2013: 7 · 2012: 2
- FWCI
- 2.58
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Journal of Clinical Microbiology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Dspace Repository (Marmara Üniversitesi) (submittedVersion, other-oa)
- Funders
- AstraZeneca
- European Society of Clinical Microbiology and Infectious Diseases
- Türkiye Bilimsel ve Teknolojik Araştırma Kurumu
- Topics
- Health Sciences › Medicine › Microbiology (medical) › Antibiotic Resistance in Bacteria
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Keywords
- Klebsiella pneumoniae, multidrug resistance, AcrAB-TolC efflux system, AcrA, OmpK35, PAβN, CCCP, quinolone resistance, chloramphenicol resistance, tetracycline resistance, beta-lactam resistance, hospital isolates, extended-spectrum beta-lactamase, Turkey
- MeSH terms
- Bacterial Outer Membrane Proteins, Bacterial Proteins, Carbonyl Cyanide m-Chlorophenyl Hydrazone, Chloramphenicol, Hydrolases, Klebsiella pneumoniae, Microbial Sensitivity Tests, Porins, Drug Resistance, Multiple, Bacterial, Escherichia coli Proteins
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