Summary: The presence of glutathione transferase (GST; EC in ATCC 25922, ATCC 25422, ATCC 8427, ATCC 27853, CIP 666, AF 101, CIP 6085, CIP 6755, and AF 2924 was investigated. Using 1-chloro-2,4-dinitrobenzene as substrate, GST activity was found in the glutathione- (GSH-) affinity-purified fraction of all strains tested. SDS-PAGE analysis of GSH-affinity-purified enzyme indicated that the GSTs of all these bacteria are dimers of two identical subunits of about 22500. Rabbit antiserum directed against the major isoenzyme present in AF 2924, Pm-GST-6·0, was used to investigate the antigenic properties of bacterial GSTs. Western blot analysis indicated that a GST antigenically identical to Pm-GST-6·0 is present in CIP 6085, ATCC 25422 and ATCC 8427, but absent in ATCC 25922, CIP 666, AF 101 and CIP 6755. The presence of Pm-GST-6·0, but not mammalian GST, increased the MIC values of amikacin, ampicillin, cefotaxime, cephalothin and nalidixic acid for ATCC 25922. It is suggested that bacterial GST may represent a defence against the effects of antibiotics.


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