Robin Frédéric, Delmas Julien, Archambaud Maryse, Schweitzer Cédric, Chanal Catherine, Bonnet Richard
CHU Clermont-Ferrand, Laboratoire de Bactériologie, Faculté de Médecine, 63 001 Clermont-Ferrand, France.
Antimicrob Agents Chemother. 2006 Jul;50(7):2403-8. doi: 10.1128/AAC.01639-05.
The clinical strain Escherichia coli TO799 was resistant to penicillin-clavulanate combinations and ceftazidime and was not reproducibly detected as an extended-spectrum beta-lactamase (ESBL) according to the standards of the Clinical Laboratory Standards Institute (CLSI; formerly NCCLS) and the national guidelines of the French Society for Microbiology (Comité de l'Antibiogramme de la Société Française de Microbiologie). A novel beta-lactamase, designated TEM-125, was responsible for this phenotype. TEM-125 harbors a complex association of mutations previously described in the ESBL TEM-12 and in the inhibitor-resistant beta-lactamase TEM-39. TEM-125 is the first complex mutant TEM to present hydrolytic activity against ceftazidime (kcat, 3.7 s(-1)) together with a high level of resistance to clavulanate (50% inhibitory concentration, 13.6 microM). The discovery of such an ESBL, which is difficult to detect by the usual ESBL detection methods, confirms the emergence of a complex mutant TEM subgroup and highlights the need to evaluate detection methods so as to avoid possible therapeutic failures.
临床菌株大肠杆菌TO799对青霉素 - 克拉维酸组合和头孢他啶耐药,并且根据临床实验室标准协会(CLSI;原NCCLS)标准和法国微生物学会国家指南(法国微生物学会抗菌谱委员会),未被重复检测为超广谱β-内酰胺酶(ESBL)。一种新型β-内酰胺酶,命名为TEM - 125,导致了这种表型。TEM - 125具有先前在ESBL TEM - 12和抑制剂耐药β-内酰胺酶TEM - 39中描述的复杂突变组合。TEM - 125是第一个对头孢他啶具有水解活性(催化常数,3.7 s(-1))同时对克拉维酸具有高耐药性(50%抑制浓度,13.6 microM)的复杂突变TEM。这种难以通过常规ESBL检测方法检测到的ESBL的发现,证实了复杂突变TEM亚组的出现,并突出了评估检测方法以避免可能的治疗失败的必要性。