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- W2156867488 abstract "ABSTRACT Although Acinetobacter baumannii is well accepted as a nosocomial pathogen, only a few of the outer membrane proteins (OMPs) have been functionally characterized. In this study, we demonstrate the biological functions of AbuO, a homolog of TolC from Escherichia coli . Inactivation of abuO led to increased sensitivity to high osmolarity and oxidative stress challenge. The Δ abuO mutant displayed increased susceptibility to antibiotics, such as amikacin, carbenicillin, ceftriaxone, meropenem, streptomycin, and tigecycline, and hospital-based disinfectants, such as benzalkonium chloride and chlorhexidine. The reverse transcription (RT)-PCR analysis indicated increased expression of efflux pumps (resistance nodulation cell division [RND] efflux pump acrD , 8-fold; SMR-type emrE homolog, 12-fold; and major facilitator superfamily [MFS]-type ampG homolog, 2.7-fold) and two-component response regulators ( baeR , 4.67-fold; ompR , 10.43-fold) in the Δ abuO mutant together with downregulation of rstA (4.22-fold) and the pilin chaperone (9-fold). The isogenic mutant displayed lower virulence in a nematode model ( P < 0.01). Experimental evidence for the binding of MerR-type transcriptional regulator SoxR to radiolabeled abuO promoter suggests regulation of abuO by SoxR in A. baumannii ." @default.
- W2156867488 created "2016-06-24" @default.
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- W2156867488 date "2015-02-01" @default.
- W2156867488 modified "2023-10-17" @default.
- W2156867488 title "AbuO, a TolC-Like Outer Membrane Protein of Acinetobacter baumannii, Is Involved in Antimicrobial and Oxidative Stress Resistance" @default.
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- W2156867488 doi "https://doi.org/10.1128/aac.03626-14" @default.
- W2156867488 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4335886" @default.
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