@article{open1669, volume = {59}, number = {2}, month = {February}, author = {Vijaya Bharathi Srinivasan and Vasanth Vaidyanathan and Govindan Rajamohan}, note = {Copyright {\copyright} 2015, American Society for Microbiology. All Rights Reserved.}, title = {AbuO, a TolC-like outer membrane protein of Acinetobacter baumannii, is involved in antimicrobial and oxidative stress resistance.}, publisher = {American Society for Microbiology}, year = {2015}, journal = {Antimicrobial agents and chemotherapy}, pages = {1236--45}, keywords = {Antimicrobial agents,Outer membrane proteins}, url = {http://crdd.osdd.net/open/1669/}, 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 {\ensuremath{\Delta}}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 {\ensuremath{\Delta}}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{\ensuremath{<}}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.} }