Presence of strA-strB gene within a streptomycin-resistance operon in a clinical isolate of shigella flexneri

Three aminoglycoside-modifying enzymes (AMEs) were produced by a clinical isolate of Shigella flexneri which was resistant to gentamicin, tobramycin, netilmicin, kanamycin, sisomicin and streptomycin: acetyltransferase (AAC) (3)-11-type, and phosphotransferase (APH) (3")- and (6)-type enzymes....

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Veröffentlicht in:Pathology 1996, Vol.28 (4), p.356-358
Hauptverfasser: Shaw, Pang-Chui, Liang, Anthony C.-T., Kam, Kai-Man, Ling, Julia M.
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Sprache:eng
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Zusammenfassung:Three aminoglycoside-modifying enzymes (AMEs) were produced by a clinical isolate of Shigella flexneri which was resistant to gentamicin, tobramycin, netilmicin, kanamycin, sisomicin and streptomycin: acetyltransferase (AAC) (3)-11-type, and phosphotransferase (APH) (3")- and (6)-type enzymes. The aminoglycoside-resistance genes were located on a 75-Kb plasmid. Two genes, strA-HK and strB-HK, in a transcriptional unit were found to code for streptomycin-resistance. The genetic organization and sequence of this transcriptional unit were identical to those of strA and strB in plasmid RSF1010. strA-HK and strB-HK when expressed separately produced functional enzymes. Our substrate profile study on the crude extracts of StrA-HK and StrB-HK proteins confirmed that StrA-HK was an APH(3")-type and showed that StrB-HK was a member of the APH(6) family.
ISSN:0031-3025
1465-3931
DOI:10.1080/00313029600169344