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Fluoroquinolone-modifying enzyme: a new adaptation of a common aminoglycoside acetyltransferase. Ari Robicsek, Jacob Strahilevitz, George A Jacoby Nature Medicine 12 , 1,January (2006) Infection disease 林建州 報告. Background. Peperazinyl substituent. AIM.

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fluoroquinolone modifying enzyme a new adaptation of a common aminoglycoside acetyltransferase

Fluoroquinolone-modifying enzyme: a new adaptation of a common aminoglycoside acetyltransferase

Ari Robicsek, Jacob Strahilevitz, George A Jacoby

Nature Medicine12, 1,January (2006)

Infection disease 林建州 報告

slide2

Background

Peperazinyl substituent

slide3

AIM

Identification of a variant of an aminoglycoside-modifying enzyme, that has acquired the ability also to modify select fluoroquinolones

result
Result
  • Identification of the resistance gene
  • Gene cloning and screening
  • Site –directed mutagenesis
  • Chemical deternination of the mechanism of resistance
  • Phenotypic testing
  • Determination of resistance-promoting potential
  • Population screening
slide5

Integron sequence of plasmid pHSH10-2.

Encoded quinolone resistance gene

slide7

Transformation

Low level ciprofloxacin resistance

slide8

Figure 1.Sequence alignment of eight different aac(6')-Ib variants and aac(6')-Ib-cr.

Try102 Arg, Asp179Try

slide11

E. coli J53 pBC SK-aac(6')-Ib-cr (. )

Figure3.Mutant prevention concentration (MPC) assay.

E. coli J53 (o )

slide12

Summary

  • We describe reduced susceptibility to ciprofloxacin in clinical bacterial isolates conferred by a variant of the gene encoding aminoglycoside acetyltransferase AAC(6')-Ib.
  • This enzyme reduces the activity of ciprofloxacin by N-acetylation at the amino nitrogen on its piperazinyl substituent
  • a single-function resistance enzyme has crossed class boundaries, and is now capable of enzymatically undermining two unrelated antimicrobial agents, one of them fully synthetic.