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Antimicrobial Agents and Chemotherapy, May 2000, p. 1229-1235, Vol. 44, No. 5
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Characterization of the Metallo-beta -Lactamase Determinant of Acinetobacter baumannii AC-54/97 Reveals the Existence of blaIMP Allelic Variants Carried by Gene Cassettes of Different Phylogeny

Maria Letizia Riccio,1 Nicola Franceschini,2 Letizia Boschi,1 Berardo Caravelli,2 Giuseppe Cornaglia,3 Roberta Fontana,3 Gianfranco Amicosante,2 and Gian Maria Rossolini1,*

Dipartimento di Biologia Molecolare, Sezione di Microbiologia, Università di Siena, I-53100-Siena,1 Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila, I-67100-L'Aquila,2 and Dipartimento di Patologia, Sezione di Microbiologia, Università di Verona, I-37134-Verona,3 Italy

Received 9 August 1999/Returned for modification 13 December 1999/Accepted 1 February 2000

The metallo-beta -lactamase determinant of Acinetobacter baumannii AC-54/97, a clinical isolate from Italy that was previously shown to produce an enzyme related to IMP-1, was isolated by means of a PCR methodology which targets amplification of gene cassette arrays inserted into class 1 integrons. Sequencing revealed that this determinant was an allelic variant (named blaIMP-2) of blaIMP found in Japanese isolates and that it was divergent from the latter by 12% of its nucleotide sequence, which evidently had been acquired independently. Similar to blaIMP, blaIMP-2 was also carried by an integron-borne gene cassette. However, the 59-base element of the blaIMP-2 cassette was unrelated to those of the blaIMP cassettes found in Japanese isolates, indicating a different phylogeny for the gene cassettes carrying the two allelic variants. Expression of the integron-borne blaIMP-2 gene in Escherichia coli resulted in a significant decrease in susceptibility to a broad array of beta -lactams (ampicillin, carbenicillin, cephalothin, cefoxitin, ceftazidime, cefepime, and carbapenems). The IMP-2 enzyme was purified from an Escherichia coli strain carrying the cloned determinant, and kinetic parameters were determined with several beta -lactam substrates. Compared to IMP-1, the kinetic parameters of IMP-2 were similar overall with some beta -lactam substrates (cefoxitin, ceftazidime, cefepime, and imipenem) but remarkably different with others (ampicillin, carbenicillin, cephaloridine, and meropenem), revealing a functional significance of at least some of the mutations that differentiate the two IMP variants. Present findings suggest that the environmental reservoir of blaIMP alleles could be widespread and raise a question about the global risk of their transfer to clinically relevant species.

* Corresponding author. Mailing address: Dipartimento di Biologia Molecolare, Sez. di Microbiologia, Università di Siena, Via Laterina, 8, 53100-Siena, Italy. Phone: 39 0577 233327. Fax: 39 0577 233325. E-mail: rossolini{at}unisi.it.

Antimicrobial Agents and Chemotherapy, May 2000, p. 1229-1235, Vol. 44, No. 5
0066-4804/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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