TY  - JOUR
N1  - Copyright © 2015, American Society for Microbiology. All Rights Reserved.
ID  - open1669
UR  - http://aac.asm.org/content/59/2/1236.abstract
IS  - 2
A1  - Srinivasan, Vijaya Bharathi
A1  - Vaidyanathan, Vasanth
A1  - Rajamohan, Govindan
Y1  - 2015/02//
N2  - 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 ?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 ?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.
PB  - American Society for Microbiology
JF  - Antimicrobial agents and chemotherapy
VL  - 59
KW  - Antimicrobial agents
KW  - Outer membrane proteins
SN  - 1098-6596
TI  - AbuO, a TolC-like outer membrane protein of Acinetobacter baumannii, is involved in antimicrobial and oxidative stress resistance.
SP  - 1236
EP  - 45
ER  -