Ceftazidime (SN401) のグラム陰性菌外膜通過性とペニシリン結合タンパク質に対する親和性

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  • CEFTAZIDIME (SN401): THE PENETRABILITY THROUGH THE OUTER MEMBRANE AND THE AFFINITY FOR THE PENICILLIN-BINDING PROTEINS OF GRAM-NEGATIVE BACTERIA
  • Ceftazidime SN401 ノ グラム インセイキン ガイマク ツウカ

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To clarify the mechanism of the strong antibacterial activities of ceftazidime (CAZ, SN 401) against Pseudomonas aeruginosa and Serratia marcescens, the penetrability through the outer membrane and the affinity to the penicillin-binding proteins were investigated with those microbes.<BR>The MICs of CAZ were not much different to the β-lactamase-free mutant and the penetrabilityincreased mutant from that to the wild strain of P. aeruginosa that produces the type lb β-lactamase chromosomally. Whereas, MICs of benzylpenicillin and cefoperazone were higher to the wild parent strain than those to the mutants. The obtained results suggest that CAZ possesses a good penetrability through the outer membrane and high stability to the β-lactamase. In fact, CAZ bound well to the PBPs of P. aeruginosa either with the whole cells or the membrane fraction, regardless of the presence of penetration barrier of the outer membrane.<BR>Since affinities to the PBPs of S. marcescens were almost same level in either CAZ or cefotaxime, it was suggested that the stronger activity of CAZ is based upon better penetrability through the outer membrane than the latter drug.

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