2006
DOI: 10.1093/jac/dkl252
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A novel ceftazidime-hydrolysing extended-spectrum  -lactamase, CTX-M-54, with a single amino acid substitution at position 167 in the omega loop

Abstract: This work shows once again that novel CTX-M enzymes with an expanded activity towards ceftazidime through a single amino acid substitution can be identified from clinical isolates. Thus, detection of CTX-M enzymes can no longer be based solely on the resistance phenotypes of clinical isolates towards ceftazidime and cefotaxime.

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Cited by 39 publications
(32 citation statements)
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“…The already-described P167S/T and D240G mutations involved in ceftazidime resistance phenotypes in natural isolates (2,6,30,36) were consistently found in our in vitro evolution experiments under ceftazidime selective pressure, as observed previously (14,22,37).…”
Section: Discussionsupporting
confidence: 88%
“…The already-described P167S/T and D240G mutations involved in ceftazidime resistance phenotypes in natural isolates (2,6,30,36) were consistently found in our in vitro evolution experiments under ceftazidime selective pressure, as observed previously (14,22,37).…”
Section: Discussionsupporting
confidence: 88%
“…The CTX-M-15 type enzyme differs from that of CTX-M-3 type by an asparagine to glycine substitution at codon 240, which leads to increased activity against ceftazidime. These CTX-M-15 type enzymes may have been selected by the increasing use of ceftazidime in clinical practice [19][20][21].…”
Section: Discussionmentioning
confidence: 99%
“…All the Salmonella isolates were examined for the presence of bla CTX-M by PCR and direct sequencing using 4 primer sets (Table 1) (18,19). The PCR reaction was performed under the following conditions: 949 C for 5 min, followed by 35 cycles of 949 C for 30 s, 609 C for 30 s, and 729 C for 30 s, with a final extension at 729 C for 5 min.…”
Section: Methodsmentioning
confidence: 99%