Ｐｒｅｖｏｔｅｌｌａ　ｉｎｔｅｒｍｅｄｉａ　ＭＡ１とＭＡ１‐Ｖ２由来β‐ｌａｃｔａｍａｓｅの基質特異性

DOI 被引用文献2件 参考文献45件

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  • Substrate profile of Prevotella intermedia MA1 and MA1-V2 .BETA.-lactamase.

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We determined the susceptibility of low level (Prevotella intermedia MA1) and high level (P. intermedia MA1-V2) β-lactamase-producers to β-lactam antibiotics and the substrate profile of β-lactamase from these organisms. Twenty-eight β-lactam antibiotics were used. MICs of four penicillins, 12 cephalosporins and two oral cephems for P. intermedia MA1-V2 were ≥128μg/ml, and β-lactamase activity from this organism against these drugs was ≥0.122 units of protein per mg. In this organism the MIC value of β-lactams paralleled the β-lactamase activity to substrate these drugs. Km and Vmax values of MA1-V2 β-lactamase against these drugs were 6.3-2, 141.7μmol and 0.03-10.21μmol/min/mg of protein, respectively. However, it seems that enzyme activity and affinity of the substrate are not associated with the MIC at all. This enzyme hydrolyzed oxyiminocephalosporins, so we concluded that the enzyme is oxyiminocephalosporinase. As cefoxitin, cefmetazole, cefbuperazon, latamoxef and imipenem inhibited the β-lactamase activity against substrate cefazolin, these drugs were stable to β-lactamase producing MA1-V2.β-Lactamase inhibitors (clavulanic acid, sulbactam and tazobactam) inhibited the activity of β-lactamase against substrate cefazolin. MICe of the β-lactam antibiotic used against MA1 were very low, and β-lactamase from this strain weakly hydrolyzed 17 substrate drugs. These results suggest that MA1-V2 β-lactamase hydrolyzes broad-spectrum β-lactam antibiotics except for cefsulodin, cephamycins, imipenem, latamoxef and aztreonam, and that this enzyme is closely associated with the cross-resistance or high level β-lactam antibiotic resistance of P. intermedia MA1-V2.

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