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Antimicrobial Agents and Chemotherapy, March 2001, p. 837-844, Vol. 45, No. 3
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.3.837-844.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Metallo-beta -Lactamase Producers in Environmental Microbiota: New Molecular Class B Enzyme in Janthinobacterium lividum

Gian Maria Rossolini,1,* Maria Adelaide Condemi,2 Fabrizio Pantanella,2 Jean-Denis Docquier,1 Gianfranco Amicosante,3 and Maria Cristina Thaller4

Dipartimento di Biologia Molecolare, Sez. di Microbiologia, Università di Siena, 53100 Siena,1 Istituto di Microbiologia, Università "La Sapienza," 00185 Rome,2 Dipartimento di Scienze e Tecnologie Biomediche, Università di L'Aquila. 67100 L'Aquila,3 and Dipartimento di Biologia, II Università di Roma "Tor Vergata," 00133 Rome,4 Italy

Received 24 July 2000/Returned for modification 27 November 2000/Accepted 21 December 2000

Eleven environmental samples from different sources were screened for the presence of metallo-beta -lactamase-producing bacteria by using a selective enrichment medium containing a carbapenem antibiotic and subsequently testing each isolate for production of EDTA-inhibitable carbapenemase activity. A total of 15 metallo-beta -lactamase-producing isolates, including 10 Stenotrophomonas maltophilia isolates, 3 Chryseobacterium spp., one Aeromonas hydrophila isolate, and one Janthinobacterium lividum isolate (a species in which production of metallo-beta -lactamase activity was not previously reported), were obtained from 8 samples. In the J. lividum isolate, named JAC1, production of metallo-beta -lactamase activity was elicited upon exposure to beta -lactams. Screening of a JAC1 genomic library for clones showing a reduced imipenem susceptibility led to the isolation of a metallo-beta -lactamase determinant encoding a new member (named THIN-B) of the highly divergent subclass B3 lineage of metallo-beta -lactamases. THIN-B is most closely related (35.6% identical residues) to the L1 enzyme of S. maltophilia and more distantly related to the FEZ-1 enzyme of Legionella gormanii (27.8% identity) and to the GOB-1 enzyme of Chryseobacterium meningosepticum (24.2% identity). Sequences related to blaTHIN-B, and inducible production of metallo-beta -lactamase activity, were also detected in the J. lividum type strain DSM1522. Expression of the blaTHIN-B gene in Escherichia coli resulted in decreased susceptibility to several beta -lactams, including penicillins, cephalosporins (including cephamycins and oxyimino cephalosporins), and carbapenems, revealing a broad substrate specificity of the enzyme. The results of this study indicated that metallo-beta -lactamase-producing bacteria are widespread in the environment and identified a new molecular class B enzyme in the environmental species J. lividum.

* 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, March 2001, p. 837-844, Vol. 45, No. 3
0066-4804/01/$04.00+0   DOI: 10.1128/AAC.45.3.837-844.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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