Reference : IND-6, a Highly Divergent IND-type Metallo-{beta}-lactamase from Chryseobacterium indolo...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/67233
IND-6, a Highly Divergent IND-type Metallo-{beta}-lactamase from Chryseobacterium indologenes strain 597 isolated in Burkina Faso.
English
Zeba, Boularé [University of Ouagadougou > Laboratoire de Chimie et de Biochimie Appliquée (UFR-SVT) > >]
De Luca, Filomena [Universita di Siena > > >]
Dubus, Alain [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Delmarcelle, Michaël mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Simporé, Jacques [> > > >]
Nacoulma, Odile G. [> > > >]
Rossolini, Gian Maria [> > > >]
Frère, Jean-Marie mailto [Université de Liège - ULg > > Centre d'ingénierie des protéines >]
Docquier, Jean-Denis [> > > >]
2009
Antimicrobial Agents and Chemotherapy
American Society for Microbiology (ASM)
Yes (verified by ORBi)
0066-4804
1098-6596
Washington
DC
[en] 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 Flavobacteriaceae, including Chryseobacterium indologenes, are naturally resistant to beta-lactam antibiotics (including carbapenems), due to the production of a resident metallo-beta-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 (that include aminoglycosides and quinolones) have been described. Here we report the identification and characterization of a new IND-type variant from a C. indologenes isolate from Burkina Faso resistant to beta-lactams and aminoglycosides. Its sequence identity with other IND-type metallo-beta-lactamases ranges from 72 to 90% (with IND-4 and IND-5, respectively). The purified enzyme exhibited N-terminal heterogeneity and a post-translational modification, consisting in 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.
http://hdl.handle.net/2268/67233
10.1128/AAC.01607-08

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