JAC Advance Access published online on January 6, 2003
Journal of Antimicrobial Chemotherapy, doi:10.1093/jac/dkg069
© 2003 by The British Society for Antimicrobial Chemotherapy
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Original article
1 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
* Corresponding author. E-mail: nordmann.patrice{at}bct.ap-hop-paris.fr.
Received 28 January 2002
; revised 12 July 2002
; accepted 29 October 2002
Flavobacterium johnsoniae CIP100931
is resistant to most
Keywords: class B Molecular and biochemical characterization of a
carbapenem-hydrolysing
-lactamase from Flavobacterium johnsoniae
-lactam antibiotics
and has a decreased susceptibility to carbapenems. A -lactamase
gene was cloned and expressed in Escherichia coli DH10B.
The purified -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 -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 -lactamases that are naturally produced
by environmental Gram-negative aerobes and that are now recognized
as the most important reservoir for these -lactamase
genes.-lactamase, Flavobacterium johnsoniae, carbapenem
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