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Please use this identifier to cite or link to this item: http://hdl.handle.net/2264/3367

Title: Identification of a novel UDP-N-acetylglucosamine enolpyruvyl transferase (MurA) from Vibrio fischeri that confers high fosfomycin resistance in Escherichia coli
Authors: Kumar, S.
Parvathi, A.
Hernandez, R.L.
Cadle, K.M.
Varela, M.F.
Citation: Archives of Microbiology, vol.191; 425-429
Issue Date: 2009
Publisher: Springer
Abstract: MurA [UDP-N-acetylglucosamine (UDP-NAG) enolpyruvyl transferase] is a key enzyme involved in bacterial cell wall peptidoglycan synthesis and a target for the antimicrobial agent fosfomycin, a structural analog of the MurA substrate phosphoenol pyruvate. In this study, it is identified that, cloned and sequenced a novel murA gene from an environmental isolate of Vibrio fischeri that is naturally resistant to fosfomycin. The fosfomycin resistance gene was isolated from a genomic DNA library of V. fischeri. An antimicrobial agent hypersensitive strain of Escherichia coli harboring murA from V. fischeri exhibited a high fosfomycin resistance phenotype, with minimum inhibitory concentration of 3,000 mu g/ml. The cloned murA gene was 1,269 bp long encoding a 422 amino acid polypeptide with an estimated pI of 5.0. The deduced amino acid sequence of the putative protein was identified as UDP-NAG enolpyruvyl transferase by homology comparison. The MurA protein with an estimated molecular weight of 44.7 kDa was expressed in E. coli and purified by affinity chromatography. MurA of V. fischeri will be a useful target to identify potential inhibitors of fosfomycin resistance in pharmacological studies
Document type: Journal Article
Copyright: An edited version of this paper was published by Springer. This paper is for R & D pupose and Copyright [2009] Springer.
URI: http://hdl.handle.net/2264/3367
Appears in Collections:Biological Sciences

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