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• W2038382077 abstract "Burkholderia pseudomallei ( Bps ) is a Gram-negative bacterium that causes melioidosis, an infectious disease of animals and humans common in northern and north-eastern parts of Thailand. Successful treatment of melioidosis is difficult due to intrinsic resistance of Bps to various antibacterial agents. It has been suggested that the antimicrobial resistance of this organism may result from poor permeability of the active compounds through porin channels located in the outer membrane (OM) of the bacterium. In previous work, a 38-kDa protein, named “ Bps Omp38”, was isolated from the OM of Bps . A topology prediction and liposome-swelling assay suggested that Bps Omp38 comprises a β-barrel structure and acts as a general diffusion porin. The present study employed black lipid membrane (BLM) reconstitution to demonstrate the single-channel conductance of the trimeric Bps Omp38 to be 2.7 ± 0.3 nS in 1 M KCl. High-time resolution BLM measurements displayed ion current blockages of seven antimicrobial agents in a concentration-dependent manner with the translocation on-rate ( k on ) following the order: norfloxacin ≫ ertapenem > ceftazidime > cefepime > imipenem > meropenem > penicillin G. The dwell time of a selected antimicrobial agent (ertapenem) decayed exponentially with increasing temperature. The energy barrier for the ertapenem binding to the affinity site inside the Bps Omp38 channel was estimated from the Arrhenius plot to be 12 kT and for the ertapenem release to be 13 kT at + 100 mV. The BLM data obtained from this study provide the first insight into antimicrobial agent translocation through the Bps Omp38 channel. ► Bps Omp38 of B. pseudomallei was reconstituted into lipid bilayers for single-channel recordings. ► The trimeric Bps Omp38 formed an ion channel with the conductance of 2.7 ± 0.3 nS in 1 M KCl. ► Flux of seven antibiotics through Bps Omp38 was analyzed and translocation on/off rates were assessed. ► The dwell time of the antibiotic ertapenem decayed exponentially with increases in temperature. ► Energy barriers obtained from Arrhenius plots suggested one affinity site inside the Omp pores." @default.
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• W2038382077 date "2011-06-01" @default.
• W2038382077 modified "2023-09-30" @default.
• W2038382077 title "Molecular analysis of antimicrobial agent translocation through the membrane porin BpsOmp38 from an ultraresistant Burkholderia pseudomallei strain" @default.
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• W2038382077 doi "https://doi.org/10.1016/j.bbamem.2010.10.018" @default.
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