Agar (Disk) Diffusion Test Susceptibility of Clinical Isolates of &lt;i&gt;Pseudomonas aeruginos&lt;/i&gt;&lt;i&gt;a&lt;/i&gt; to Azlocillin, Cefotaxime, Cefsulodin, Lamoxactam, Mezlocillin, and Piperacillin

Traub, Walter H.

doi:10.1159/000238087

Cited by 3 publications

(2 citation statements)

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“…To assess the alteration in drug efflux function of the gene knockout strain and identify drugs with efflux effects, we employed the micro broth dilution method and drug susceptibility disk detection as outlined by Traub and Tarpay et al [33,34] . This allowed us to observe changes in drug sensitivity between knockout and anaplerotic strains.…”

Section: Drug Sensitivity Testsmentioning

confidence: 99%

Functional characterization of the Escherichia coli membrane transport protein MdtEF

Tong,

Liang,

Liu

et al. 2024

Preprint

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The mdtE and mdtF genes encode membrane transporters, with their transport substrates and mechanisms still not fully understood. Amino acid sequence analysis suggests that MdtE belongs to the MFP family while MdtF belongs to the RND family. MdtF is positioned in the inner membrane, while MdtE is found in the periplasmic space, connecting MdtF with the outer membrane porin TolC to create a MdtEF-TolC tripartite efflux pump for drug and substrate efflux. Subsequently, an Escherichia coli (E. coli) mdtEF gene deletion strain was developed using a suicide plasmid method. An expression vector, was then constructed and complemented based on the pBR322 vector. Drug sensitivity tests and EB accumulation experiments were performed on the mdtEF gene deletion strain, revealing that the MdtEF protein could efflux the carbapenems imipenem and ertapenem. In the EB accumulation experiment, two inhibitors, vanadate and carbonyl m-chlorophenylhydrazone (CCCP), were utilized, demonstrating that MdtEF functions through the proton gradient's potential energy for substrate transport.

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Section: Drug Sensitivity Testsmentioning

confidence: 99%

Functional characterization of the Escherichia coli membrane transport protein MdtEF

Tong,

Liang,

Liu

et al. 2024

Preprint

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“…According to the method of Traub et al and Biswas et al [26][27][28], WT E. coli and three mutant strains were tested for drug sensitivity with norfloxacin susceptibility discs. Cells were cultured in LB solid medium with norfloxacin susceptibility discs and grown at 37 o C for 24 h. Diameters of inhibition zones were measured with Vernier calipers.…”

Section: Drug Susceptibility Assaysmentioning

confidence: 99%

Cloning and Functional Characterization of Putative Escherichia coli ABC Multidrug Efflux Transporter YddA

Feng¹,

Liu²,

Liu³

et al. 2020

J. Microbiol. Biotechnol.

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/nodulation/cell division (RND), the proteobacterial antimicrobial compound efflux (PACE) family and the p-aminobenzoyl-glutamate transporter (AbgT) family [1]. Of these, SMR, MFS, MATE, RND, PACE and AbgT use proton kinetic potential as energy and ABC transporters use ATP as energy. All of them can export drugs and other substrates out of cells [2]. Some proteins, although they confer low levels of resistance, are often the first step in resistance, eventually leading to higher resistance by acquiring chromosomal mutations that target antibiotics. The ABC transporter is one of these proteins [3]. ABC transporters exist in almost all organisms from microorganisms to humans [4, 5]. ABC transporters have attracted extensive attention because of their involvement in important physiological processes such as bacterial resistance, human cystic fibrosis, and tumor cell resistance to chemotherapy drugs [6]. ABC transporters contain similar topologies, with two transmembrane domains (TMD) and two nucleotide-binding domains (NBD). These four domains can fuse to form a full transporter such as the multidrug efflux pump P-glycoprotein (P-gp, ABCB1 or MDR1) in humans. In bacteria, multidrug efflux pumps usually fuse to form a half-transporter with a TMD and an NBD domain [7]. The half-transporter forms a homodimer such as MsbA [7] or LmrA [8]. It can also form heterodimers such as EfrCD [9], YheI/YheH [10] and PatA/PatB [11]. The E. coli K-12MG1655 strain genome was predicted to encode 69 ABC transporters. Eleven of the ABC transporters are presumed to be exporters [5, 12]. Efflux systems of the ABC family in E. coli were reported to mainly include capsular polysaccharide transport pump KpsT [13], hemolysin transport pump HlyA [14, 15], macrocyclic lipid drug efflux pump MacAB [16], outer membrane lipoprotein transport pump LolACDE [17-19], multidrug resistance and phospholipid A transporter MsbA [20], micromycin J25 efflux pump YojI [21], and heme efflux pump CcmABC [22]. Drug efflux systems in E. coli that have been reported included MsbA and MacA. MsbA is a multidrug efflux pump and MacAB is a single-drug efflux pump of macrolides[16]. Studies reported on the A putative multidrug efflux gene, yddA, was cloned from the Escherichia coli K-12 strain. A drugsensitive strain of E. coli missing the main multidrug efflux pump AcrB was constructed as a host and the yddA gene was knocked out in wild-type (WT) and drug-sensitive E. coliΔacrB to study the yddA function. Sensitivity to different substrates of WT E.coli, E. coliΔyddA, E. coliΔacrB and E. coliΔacrBΔyddA strains was compared with minimal inhibitory concentration (MIC) assays and fluorescence tests. MIC assay and fluorescence test results showed that YddA protein was a multidrug efflux pump that exported multiple substrates. Three inhibitors, ortho-vanadate, carbonyl cyanide m-chlorophenylhydrazone (CCCP), and reserpine, were used in fluorescence tests. Ortho-vanadate and reserpine significantly inhibited the efflux and increased accumulation of ethidium bromide and norf...

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Cefsulodin in der Therapie der Pseudomonasmeningitis

Brückner

Collmann

Trautmann³

1983

Infection

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Three patients with meningitis due to Pseudomonas aeruginosa (in one patient following a neurosurgical procedure and in two patients following severe head trauma with multiple skull bone fractures and liquorrhea) were treated with cefsulodin in combination with other antibiotics (aminoglycosides/acylureido penicillins). All of the patients were cured. Two patients received intraventricular administrations of aminoglycosides in addition to systemically applied antibiotics. After recurrence of pseudomonas meningitis in one patient in spite of the intraventricular application of an aminoglycoside, definite cure could only be obtained by additional intraventricular application of cefsulodin. The third patient was cured by systemic administration of cefsulodin and amikacin. The value of cefsulodin is discussed with reference to obtainable ventricular and lumbar CSF concentrations.

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Agar (Disk) Diffusion Test Susceptibility of Clinical Isolates of <i>Pseudomonas aeruginos</i><i>a</i> to Azlocillin, Cefotaxime, Cefsulodin, Lamoxactam, Mezlocillin, and Piperacillin

Cited by 3 publications

References 4 publications

Functional characterization of the Escherichia coli membrane transport protein MdtEF

Functional characterization of the Escherichia coli membrane transport protein MdtEF

Cloning and Functional Characterization of Putative Escherichia coli ABC Multidrug Efflux Transporter YddA

Cefsulodin in der Therapie der Pseudomonasmeningitis

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