Chouchani Chedly, Ben-Achour Nahed, M'charek Arij, Belhadj Omrane
Laboratoire de biochimie et de biotechnologie, faculté des sciences de Tunis, 2092 El-Manar II, Tunisia.
C R Biol. 2007 Aug;330(8):565-70. doi: 10.1016/j.crvi.2007.03.017. Epub 2007 May 17.
A clinical isolate of Escherichia coli LBT04 was found to have a high-level resistance to broad-spectrum beta-lactams. Analysis of this strain by the disk diffusion test revealed synergies between clavulanic acid and ceftazidime, cefotaxime. Clavulanic acid decreased the MICs of ceftazidime, cefotaxime, and ceftriaxone, which suggested that LBT04 produced an extended-spectrum beta-lactamase. These resistances were carried by a 1080-bp chromosomal gene that encoded a beta-lactamase with a pI of 6.3. Cloning and sequencing experiments showed that this beta-lactamase revealed identity with the bla(TEM-1) gene encoding the TEM-1 beta-lactamase, except for a replacement of the Glu residue at position 104 by Lys, and of the Gly residue at position 238 by Ser. These two mutations were encountered in TEM-15 beta-lactamase, but this is the first description of this enzyme in the E. coli species in Tunisian hospitals.
一株临床分离的大肠杆菌LBT04被发现对广谱β-内酰胺类药物具有高水平耐药性。通过纸片扩散法对该菌株进行分析,发现克拉维酸与头孢他啶、头孢噻肟之间存在协同作用。克拉维酸降低了头孢他啶、头孢噻肟和头孢曲松的最低抑菌浓度(MIC),这表明LBT04产生了超广谱β-内酰胺酶。这些耐药性由一个1080碱基对的染色体基因携带,该基因编码一种pI为6.3的β-内酰胺酶。克隆和测序实验表明,这种β-内酰胺酶与编码TEM-1β-内酰胺酶的bla(TEM-1)基因具有同一性,只是第104位的Glu残基被Lys取代,第238位的Gly残基被Ser取代。这两个突变在TEM-15β-内酰胺酶中出现过,但这是该酶在突尼斯医院的大肠杆菌中首次被描述。