Journal of Antimicrobial Chemotherapy (1994) 33, 707-720
© 1994 The British Society for Antimicrobial Chemotherapy
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Convergent evolution of TEM-26, a ß-lactamase with extended-spectrum activity
aDepartment of Microbiology, University of Leeds Leeds LS2 9JT, UK bDepartment of Microbiology, St James's University Hospital Leeds LS2 9TE, UK
Received 2 August 1993; accepted 23 November 1993
*Correspondence to: Professor P. M. Hawkey, Department of Microbiology, University of Leeds, Leeds LS2 9JT, UK
TEM-26, an extended-spectrum ß-lactamase has been characterized in clinical isolates of Klebsiella pneumoniae and Escherichia coli derived from patients on the Paediatric Oncology Unit of St James's University Hospital, Leeds. The nucleotide sequence of this ß-lactamase gene (blaTEM26b) was determined, and compared with the nucleotide sequences of other TEM-type ß-lactamases. The blaTEM26b, gene was found to differ from blaTEM12b by a single nucleotide. This difference causes the substitution of glutamic acid in blaTEM26b for lysine in blaTEM26b at position 102 in the predicted amino acid sequence. The blaTEM12b gene was first described in an isolate of Klebsiella oxytoca from a patient nursed on the same unit that yielded the strains that carry blaTEM26b However, the blaTEM26b gene differs at no less than six nucleotides from the nucleotide sequence encoding the TEM-26 ß-lactamase that was first described in isolates from cancer patients nursed in the Children's Hospital, Stanford, California, USA. This indicates that the genes encoding TEM-26 have evolved from different progenitors.
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