Author:
Srinivasan Vijaya Bharathi,Vaidyanathan Vasanth,Rajamohan Govindan
Abstract
ABSTRACTAlthoughAcinetobacter baumanniiis 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 fromEscherichia coli. Inactivation ofabuOled to increased sensitivity to high osmolarity and oxidative stress challenge. The ΔabuOmutant 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 pumpacrD, 8-fold; SMR-typeemrEhomolog, 12-fold; and major facilitator superfamily [MFS]-typeampGhomolog, 2.7-fold) and two-component response regulators (baeR, 4.67-fold;ompR, 10.43-fold) in the ΔabuOmutant together with downregulation ofrstA(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 radiolabeledabuOpromoter suggests regulation ofabuOby SoxR inA. baumannii.
Publisher
American Society for Microbiology
Subject
Infectious Diseases,Pharmacology (medical),Pharmacology
Cited by
41 articles.
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