Abstract
An ABC transporter gene from Clostridium hathewayi is characterized. It has duplicated ATPase domains in addition to a transmembrane protein. Its deduced amino acid sequence has conserved functional domains with ATPase components of the multidrug efflux pump genes of several bacteria. Cloning this transporter gene into C. perfringens and E. coli resulted in decreased sensitivities of these bacteria to fluoroquinolones. It also decreased the accumulation and increased the efflux of ethidium bromide from cells containing the cloned gene. Carbonyl cyanide-m-chlorophenylhydrazone (CCCP) inhibited both accumulation and efflux of ethidium bromide from these cells. The ATPase mRNA was overexpressed in the fluoroquinolone-resistant strain when exposed to ciprofloxacin. This is the first report of an ABC transporter in C. hathewayi.







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We thank John B. Sutherland and Carl E. Cerniglia for comments on the manuscript and research support. The views presented in this article do not necessarily reflect those of the US Food and Drug Administration.
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Communicated by Wolfgang Buckel.
An erratum to this article can be found at http://dx.doi.org/10.1007/s00203-008-0411-5
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Rafii, F., Park, M. Detection and characterization of an ABC transporter in Clostridium hathewayi . Arch Microbiol 190, 417–426 (2008). https://doi.org/10.1007/s00203-008-0385-3
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DOI: https://doi.org/10.1007/s00203-008-0385-3