Silver Resistance In Acinetobacter baumannii BL54 Occurs Through Binding to a Ag-Binding Protein


1 Department Of Genetics, Research Center, Kerman University of Medical sciences, Kerman, Iran.

2 Department Of Microbiology, University Of Pune, Pune 114700, India.


The mechanism of plasmid mediated silver (Ag) resistance was investigated in Acinetobacter baumannii
BL54. The intracellular accumulation of Ag in both original strain BL54 and Escherichia coli K12
transconjugant containing plasmid pUPI276 began immediately and reached a maximum within 60 minutes.
This initial accumulation was followed by net loss of Ag which reached a maximum within 180 min.
Pre-treatment of cells with 0.5 mM 2,4 dinitrophenol (DNP); 20 mM N, N-dicyclohexylcarbodiimide
(DCCD); 3% toluene; 25 mg/ml cefotaxime and polymyxin-B resulted in considerable decrease in the
accumulation process. Ags plasmid less cured derivative (BL54.1) also accumulated silver but only onefourth
the amount compared to the resistant strain BL54. The intracellular accumulated silver is detoxified
by binding to a cysteine rich metal binding protein.
The purified Ag-binding protein exhibited maximum absorption at 280/215 nm. From the above data
it could be concluded that the intracellular detoxification of silver in A. baumannii BL54 is achieved
through binding to a cysteine rich metalloprotein.