Susceptibility of Pseudomonas aeruginosa Isolates to Ceftazidime Is Unrelated to the Expression of the Outer Membrane Protein OprC

Perez, Federico; Navarro, David; Gimeno, C.; García‐de‐Lomas, Juan

doi:10.1159/000239531

Cited by 4 publications

(4 citation statements)

References 6 publications

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“…Sobel et al found that disruption of the PA2491 gene of this bacterium increased expression of the MexEF−OprN multidrug efflux genes and decreased production of outer membrane protein OprD, concomitant with enhanced resistance to chloramphenicol, quinolones, and imipenem, which was reminiscent of previously described NfxC mutants , These reports suggest that Omp proteome instead of one Omp plays an important role in P. aeruginosa resistance to antibiotics. …”

Section: Introductionmentioning

confidence: 75%

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Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Pseudomonas aeruginosa Responding to Ampicilin, Kanamycin, and Tetracycline Resistance

Peng

Ren

et al. 2005

J. Proteome Res.

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Nosocomial wound infections by antibiotic-resistant Pseudomonas aeruginosa strains have increasing importance in hospitals. Outer membrane proteins of the bacterium have strong influence on its resistance to antibiotics. In the current study, a parallel proteomic approach was applied to analysis of sarcosine-insoluble outer membrane fraction of P. aeruginosa responding to ampicilin, kanamycin and tetracycline resistances. Eleven differential proteins with 15 spots were determined and then identified by MALDI-TOF/MS, in which four with increased OprF, MexA, OmpH, and decreased hypothetical protein (NCBI No. 15599856), six with increased OprF, OmpH, hypothetical protein (NCBI No. 15599183) and decreased OprG, MexA, conserved hypothetical protein (NCBI No. 15600371), and eight with increased OprF, MexA, OprL, probable Omp (NCBI No. 15599856), probable secretion protein (NCBI No. 15600167), OprD and decreased OprG, conserved hypothetical protein (NCBI No. 15600371) responded to ampicilin, kanamycin, and tetracycline resistances, respectively. With the exception of OprF, the other differential proteins did not show the same behaviors against the three antibiotic resistances. Compared with our previous report on E. coli Omps responding to ampicilin and tetracycline resistances, which was only a protein difference in quality between the two antibiotics, P. aeruginosa showed significant diversity against the three antibiotics. Our findings might provide valuable data for an understanding of antibiotic-resistant difference between different species of bacteria. Meanwhile, these proteins shared by different bacteria or a bacterium against different antibiotics may provide universal targets for the development of new drugs that control antibiotic-resistant bacteria.

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Section: Introductionmentioning

confidence: 75%

“…15 Moreover, other porins including OprF, OprE, and OprD showed the importance of antibiotic resistance in this bacterium. 16,17 These reports suggest that Omp proteome instead of one Omp plays an important role in P. aeruginosa resistance to antibiotics.…”

Section: Introductionmentioning

confidence: 99%

Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Pseudomonas aeruginosa Responding to Ampicilin, Kanamycin, and Tetracycline Resistance

Peng

Ren

et al. 2005

J. Proteome Res.

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“…It has been shown in outer-membrane diffusion studies that OprD is the principal portal of entry for imipenem (Huang & Hancock, 1996;Perez et al, 1996). Confirming these experiments, imipenem-resistant isolates, in some studies, have been found to be deficient in the OprD protein (Trias et al, 1989;Yoneyama & Nakae, 1993).…”

Section: Discussionmentioning

confidence: 79%

Effect of carbapenems on the transcriptional expression of the oprD, oprM and oprN genes in Pseudomonas aeruginosa

Kolayli¹,

Karadenizli²,

Savlı³

et al. 2004

Journal of Medical Microbiology

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The effects of imipenem and meropenem on the transcriptional expression of resistance-related genes oprD, oprM and oprN in Pseudomonas aeruginosa were studied by quantitative real-time PCR. Four strains were examined: the type strain PT5 (PAO1), its derivatives M7 and PT149, and a clinical isolate, PaKT3. The derivative M7 is a nalB mutant, overexpressing the MexAB-OprM pump, and the derivative PT149 is a nfxC-type mutant, overexpressing the MexEF-OprN pump while it is down-regulated for the OprD protein. After 18 h incubation in broth, the cultures were divided into three portions. Two were supplemented with antibiotics and the other was left antibiotic-free as the control. After a further 45 min incubation, total RNA was isolated from the strains by guanidine denaturation and acid-phenol/chloroform extraction. DNA-free total RNAs were immediately reverse-transcribed by MMuLV reverse transcriptase. Concentrations of mRNAs obtained by quantitative PCR were expressed relative to uninduced portions of the strains. The results showed that oprD was relatively stable against carbapenem antibiotics. oprM was induced significantly by imipenem in only one strain and oprN was induced by imipenem in most of the strains. The responses at the mRNA level found here were unexpected and suggested a chaotic, unpredictable regulatory mechanism.

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“…OprC is one of the outer membrane porins responsible for channel-forming and copper binding (11). Then, researchers focused on the relationship between MDR and OprC in P. aeruginosa and revealed (12)(13)(14) that OprC was unrelated to meropenem, ceftazidime susceptibility, and imipenem diffusion.…”

Section: Introductionmentioning

confidence: 99%

oprC Impairs Host Defense by Increasing the Quorum-Sensing-Mediated Virulence of Pseudomonas aeruginosa

Gao

Guo

et al. 2020

Front. Immunol.

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Pseudomonas aeruginosa, found widely in the wild, causes infections in the lungs and several other organs in healthy people but more often in immunocompromised individuals. P. aeruginosa infection leads to inflammasome assembly, pyroptosis, and cytokine release in the host. OprC is one of the bacterial porins abundant in the outer membrane vesicles responsible for channel-forming and copper binding. Recent research has revealed that OprC transports copper, an essential trace element involved in various physiological processes, into bacteria during copper deficiency. Here, we found that oprC deletion severely impaired bacterial motility and quorum-sensing systems, as well as lowered levels of lipopolysaccharide and pyocyanin in P. aeruginosa. In addition, oprC deficiency impeded the stimulation of TLR2 and TLR4 and inflammasome activation, resulting in decreases in proinflammatory cytokines and improved disease phenotypes, such as attenuated bacterial loads, lowered lung barrier damage, and longer mouse survival. Moreover, oprC deficiency significantly alleviated pyroptosis in macrophages. Mechanistically, oprC gene may impact quorum-sensing systems in P. aeruginosa to alter pyroptosis and inflammatory responses in cells and mice through the STAT3/NF-κB signaling pathway. Our findings characterize OprC as a critical virulence regulator, providing the groundwork for further dissection of the pathogenic mechanism of OprC as a potential therapeutic target of P. aeruginosa.

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Susceptibility of Pseudomonas aeruginosa Isolates to Ceftazidime Is Unrelated to the Expression of the Outer Membrane Protein OprC

Cited by 4 publications

References 6 publications

Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Pseudomonas aeruginosa Responding to Ampicilin, Kanamycin, and Tetracycline Resistance

Proteomic Analysis of the Sarcosine-Insoluble Outer Membrane Fraction of Pseudomonas aeruginosa Responding to Ampicilin, Kanamycin, and Tetracycline Resistance

Effect of carbapenems on the transcriptional expression of the oprD, oprM and oprN genes in Pseudomonas aeruginosa

oprC Impairs Host Defense by Increasing the Quorum-Sensing-Mediated Virulence of Pseudomonas aeruginosa

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