Journal of Antimicrobial Chemotherapy (1992) 30, 449-462
© 1992 The British Society for Antimicrobial Chemotherapy
research-article |
Clinical isolates of Escherichia coli producing TRI ß-lactamases: novel TEM-enzymes conferring resistance to ß-lactamase inhibitors
aLaboratoire de Bactériologie CHU Cochin 24, rue du Faubourg Saint-Jacques, 75014 Paris bMuséum National d'Histoire Naturelle CNRS UA 401, 63, rue Buffon, 75231 Paris Cedex 05, France
Received 31 October 1991; returned 20 May 1992; accepted 20 May 1992
Two different strains of Eschtrichia coli exhibiting unusual patterns of resistance to ß-lactam antibiotics were isolated from patients at Cochin Hospital. Both isolates showed a low level of resistance to amoxycillin, ticarcillin and ureidopenicillins but were susceptible to ccphalosporins, aztreonam and imipenem; ß-lactamase inhibitors potentiated the activities of the ß-lactams to only a limited extent All resistance characteristics of the strains were transferable by conjugation to E. coli K12. Resistance was shown to be due to ß-lactamases of pI 5·20 and relative molecular masses of 24,000 . The hydrolytic and inhibition profiles of these enzymes were similar to each other but differed from those of broad-spectrum ß-lactamases (TEM-I). The rates of hydrolysis (Vmax)of amoxycillin (c. 200%) were higher than that for TEM-1 (84%). Ticarcillin, ureidopenicillins and cephaloridine were hydrolyzed slowly. However, as for TEM-1, no hydrolysis was observed with cefoxitin, third generation ccphalosporins, aztreonam and imipenem. The high Km values demonstrated the poor affinity of these enzymes for their substrates. Unlike TEM-1, they were poorly inhibited by ß-lactamase inhibitors. These two enzymes differed from each other as follows: (i) the concentrations of clavulanic acid required for 50% ß-lactamase inhibition were 31 µmol/L for one enzyme (E-SAL) and 9·4 µmol/L for the other (E-GUER); (ii) p-cbloromercuribenzoate was a more active inhibitor of E-SAL then E-GUER. The titration curve method and DNA-DNA hybridization studies demonstrated that both enzymes were structurally related to TEM-1. The novel plasmid-encoded enzymes produced by the two isolates of E. coli appeared to be almost identical and to be derived from TEM-enzymes. On the basis of their presumed phytogeny and their biological properties, we propose that these ß-lactamases be given the generic name TRI (TEM Resistant to ß-lactamase Inhibitors).
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