Bret L, Chaibi E B, Chanal-Claris C, Sirot D, Labia R, Sirot J
Laboratoire de Bactériologie, Faculté de Médecine, Clermont-Ferrand, France.
Antimicrob Agents Chemother. 1997 Nov;41(11):2547-9. doi: 10.1128/AAC.41.11.2547.
A novel inhibitor-resistant TEM (IRT) beta-lactamase was detected in an Escherichia coli isolate resistant to amoxicillin-clavulanate and susceptible to cephalothin. The substrate and inhibitor profiles of this beta-lactamase were similar to those of IRT-1 and IRT-2. The novel IRT's bla gene was sequenced, and the deduced amino acid sequence showed the amino acid replacement Arg for His-244 of the TEM-1 sequence. Substitutions for Arg-244 have been reported in three TEM-1 mutants: IRT-1 (which corresponds to TEM-31) (Cys), IRT-2/TEM-30 (Ser), and TEM-41 (Thr). We designated this novel beta-lactamase, which corresponds to TEM-51, IRT-15.
在一株对阿莫西林-克拉维酸耐药但对头孢噻吩敏感的大肠埃希菌分离株中检测到一种新型的抑制剂耐药性TEM(IRT)β-内酰胺酶。该β-内酰胺酶的底物和抑制剂谱与IRT-1和IRT-2相似。对该新型IRT的bla基因进行了测序,推导的氨基酸序列显示在TEM-1序列的His-244位点发生了氨基酸替换,由精氨酸取代。在三个TEM-1突变体中已报道了Arg-244的替换:IRT-1(对应于TEM-31)(半胱氨酸)、IRT-2/TEM-30(丝氨酸)和TEM-41(苏氨酸)。我们将这种对应于TEM-51的新型β-内酰胺酶命名为IRT-15。