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Antimicrobial Agents and Chemotherapy, October 2009, p. 4320-4326, Vol. 53, No. 10
0066-4804/09/$08.00+0     doi:10.1128/AAC.01607-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

IND-6, a Highly Divergent IND-Type Metallo-β-Lactamase from Chryseobacterium indologenes Strain 597 Isolated in Burkina Faso {triangledown}

Boukaré Zeba,1 Filomena De Luca,2 Alain Dubus,3 Michael Delmarcelle,3 Jacques Simporé,1,4 Odile G. Nacoulma,1 Gian Maria Rossolini,2 Jean-Marie Frère,3 and Jean-Denis Docquier2*

Laboratoire de Chimie et de Biochimie Appliquée (UFR-SVT), University of Ouagadougou, 03 BP 7021 Ouagadougou, Burkina Faso,1 Dipartimento di Biologia Molecolare, Laboratorio di Fisiologia e Biotecnologia dei Microrganismi, Università di Siena, I-53100 Siena, Italy,2 Centre d'Ingénierie des Protéines et Laboratoire d'Enzymologie, Université de Liège, B-4000 Liège, Belgium,3 Saint Camille Medical Center, 01 BP 364 Ouagadougou, Burkina Faso4

Received 4 December 2008/ Returned for modification 16 April 2009/ Accepted 24 July 2009

The genus Chryseobacterium and other genera belonging to the family Flavobacteriaceae include organisms that can behave as human pathogens and are known to cause different kinds of infections. Several species of Flavobacteriaceae, including Chryseobacterium indologenes, are naturally resistant to β-lactam antibiotics (including carbapenems), due to the production of a resident metallo-β-lactamase. Although C. indologenes presently constitutes a limited clinical threat, the incidence of infections caused by this organism is increasing in some settings, where isolates that exhibit multidrug resistance phenotypes (including resistance to aminoglycosides and quinolones) have been detected. Here, we report the identification and characterization of a new IND-type variant from a C. indologenes isolate from Burkina Faso that is resistant to β-lactams and aminoglycosides. The levels of sequence identity of the new variant to other IND-type metallo-β-lactamases range between 72 and 90% (for IND-4 and IND-5, respectively). The purified enzyme exhibited N-terminal heterogeneity and a posttranslational modification consisting of the presence of a pyroglutamate residue at the N terminus. IND-6 shows a broad substrate profile, with overall higher turnover rates than IND-5 and higher activities than IND-2 and IND-5 against ceftazidime and cefepime.

* Corresponding author. Mailing address: Dipartimento di Biologia Molecolare, Università di Siena, Policlinico Le Scotte, I-53100 Siena, Italy. Phone: 39 0577 233134. Fax: 39 0577 233870. E-mail: jddocquier{at}unisi.it

{triangledown} Published ahead of print on 3 August 2009.

Antimicrobial Agents and Chemotherapy, October 2009, p. 4320-4326, Vol. 53, No. 10
0066-4804/09/$08.00+0     doi:10.1128/AAC.01607-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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