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Characterization of a new extended-spectrum beta-lactamase (TEM-87) isolated in Proteus mirabilis during an Italian survey.

ABSTRACT: A new natural TEM derivative, named TEM-87, was identified in a Proteus mirabilis isolate from an Italian hospital. Compared to TEM-1, TEM-87 contains the following mutations: E104K, R164C, and M182T. Kinetic analysis of TEM-87 revealed extended-spectrum activity against oxyimino cephalosporins (preferentially ceftazidime) and aztreonam. Expression of blaTEM-87 in Escherichia coli decreased the host susceptibility to these drugs.

SUBMITTER: Perilli M

PROVIDER: S-EPMC127476 | biostudies-literature | 2002 Mar

REPOSITORIES: biostudies-literature

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Characterization of a new extended-spectrum beta-lactamase (TEM-87) isolated in Proteus mirabilis during an Italian survey.

Perilli Mariagrazia M Segatore Bernardetta B De Massis Maria Rosaria MR Franceschini Nicola N Bianchi Ciro C Rossolini Gian Maria GM Amicosante Gianfranco G

Antimicrobial agents and chemotherapy 20020301 3

A new natural TEM derivative, named TEM-87, was identified in a Proteus mirabilis isolate from an Italian hospital. Compared to TEM-1, TEM-87 contains the following mutations: E104K, R164C, and M182T. Kinetic analysis of TEM-87 revealed extended-spectrum activity against oxyimino cephalosporins (preferentially ceftazidime) and aztreonam. Expression of blaTEM-87 in Escherichia coli decreased the host susceptibility to these drugs. ...[more]

PMID: 11850290

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