<i>In vitro</i> and <i>in vivo</i> Transferrable β-Lactam Resistance Due to a New Plasmid-Mediated Oxyiminocephalosporinase from a Clinical Isolate of <i>Proteus mirabilis</i>

J-STAGE
  • WATANABE Yuji
    Department of Bacteriology, Juntendo University School of Medicine
  • YOKOTA Takeshi
    Department of Bacteriology, Juntendo University School of Medicine
  • HIGASHI Yasuyuki
    Product Development Laboratories, Fujisawa Pharmaceutical Co., Ltd.
  • WAKAI Yoshimi
    Product Development Laboratories, Fujisawa Pharmaceutical Co., Ltd.
  • MINE Yasuhiro
    Product Development Laboratories, Fujisawa Pharmaceutical Co., Ltd.

抄録

A new plasmid-mediated β-lactamase (FPM-1) with an isoelectric point of 7.2 and a molecular weight of 26, 000 was found in a cefuroxime-resistant clinical isolate of Proteus mirabilis strain 6003. FPM-1 can be classified as a type I oxyiminocephalosporinase on the basis of its substrate specificity and inhibition pattern by clavulanic acid etc., and it conferred resistance on both the strain and transconjugants against most oxyme-type cephalosporins as well as the older ones but not against cefamycins and a few exceptional oxyme-type cephalosporins such as ceftizoxime, ceftazidime and cefixime. In a murine systemic infection model, only these FPM-1-stable drugs exhibited protective activity against the FPM-1-producing P. mirabilis 6003 similar to that against a nonproducing derivative strain. The FPM-1-mediated cefuroxime resistance in P. mirabilis 6003 was transferred to co-infected Escherichia coli 7004 at frequencies between 3.8×10-3 and 4.0×10-2 in a murine ascending urinary tract infection model. In the same infection model due to the FPM-1-producing E. coli transconjugant, FPM-1-stable cefixime was significantly more effective than FPM-1-labile cefteram pivoxil, although both drugs had similar therapeutic effect against its FPM-1-nonproducing counterpart strain.

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