JAC Advance Access originally published online on January 6, 2003
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Journal of Antimicrobial Chemotherapy (2003) 51, 267-273
© 2003 The British Society for Antimicrobial Chemotherapy
Molecular and biochemical characterization of a carbapenem-hydrolysing ß-lactamase from Flavobacterium johnsoniae
Service de Bactériologie-Virologie, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine Paris-Sud, 78 rue du Général Leclerc, 94275 Le Kremlin-Bicêtre Cédex, France
Received 28 January 2002; returned 12 July 2002; revised 25 July 2002; accepted 29 October 2002
Flavobacterium johnsoniae CIP100931 is resistant to most ß-lactam antibiotics and has a decreased susceptibility to carbapenems. A ß-lactamase gene was cloned and expressed in Escherichia coli DH10B. The purified ß-lactamase, JOHN-1, with a pI value of 9.0 and with a determined relative molecular mass of 
27 kDa was found to be a monomeric zinc-dependent enzyme that hydrolyses penicillins, narrow- and expanded-spectrum cephalosporins, carbapenems, but not monobactams. Sequence analysis revealed that JOHN-1 is a molecular class B ß-lactamase that is most closely related to BlaB from Chryseobacterium meningosepticum and IND-1 from Chryseobacterium indologenes (47% and 41% amino acid identity, respectively). JOHN-1 is a new member of the highly divergent subclass B1 lineage of metallo-enzymes. Although F. johnsoniae and Chryseobacterium spp. are phylogenetically related bacteria, this report further underlines the heterogeneity of class B ß-lactamases that are naturally produced by environmental Gram-negative aerobes and that are now recognized as the most important reservoir for these ß-lactamase genes.
Keywords: class B ß-lactamase, Flavobacterium johnsoniae, carbapenem
* Corresponding author. Tel: +33-1-45-21-36-32; Fax: 33-1-45-21-63-40; E-mail: nordmann.patrice{at}bct.ap-hop-paris.fr
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