JAC Advance Access originally published online on May 29, 2003
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Journal of Antimicrobial Chemotherapy (2003) 52, 29-35
© 2003 The British Society for Antimicrobial Chemotherapy
Effect of D240G substitution in a novel ESBL CTX-M-27
1 Laboratoire de Bactériologie, Faculté de Médecine, Service de Bactériologie-Virologie, 28 Place Henri-Dunant, 63001 Clermont-Ferrand Cedex; 2 Laboratoire de Bactériologie, CHU de Grenoble, Chemin Maquis du Grésivaudan, 38 700 La Tronche, France
Received 27 January 2003; returned 14 February 2003; revised 13 March 2003; accepted 13 March 2003
Escherichia coli clinical strain Gre-1 collected in 2000 from a French hospital harboured a novel CTX-M-encoding gene, designated blaCTX-M-27. CTX-M-27 differed from CTX-M-14 only by the substitution D240G and was the third CTX-M enzyme harbouring this mutation after CTX-M-15 and CTX-M-16. The Gly-240-harbouring enzyme CTX-M-27 conferred to E. coli higher MICs of ceftazidime (MIC, 8 versus 1 mg/L) than did the Asp-240-harbouring CTX-M-14 enzyme. Comparison of CTX-M-14 and CTX-M-27 showed that residue Gly-240 decreased Km for ceftazidime (205 versus 940 µM), but decreased hydrolytic activity against good substrates, such as cefotaxime (kcat, 113 versus 415 s–1), probably owing to the alteration of ß3 strand positioning during the catalytic process.
Keywords: CTX-M, ß-lactamase, D240G mutation, ESBL
* Corresponding author. Fax: +33-4-73-27-74-94; E-mail: Richard.Bonnet{at}u-clermont1.fr
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