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IND-6, a highly divergent IND-type metallo-beta-lactamase from Chryseobacterium indologenes strain 597 isolated in Burkina Faso.
- Source :
-
Antimicrobial agents and chemotherapy [Antimicrob Agents Chemother] 2009 Oct; Vol. 53 (10), pp. 4320-6. Date of Electronic Publication: 2009 Aug 03. - Publication Year :
- 2009
-
Abstract
- 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 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 (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 beta-lactams and aminoglycosides. The levels of sequence identity of the new variant to other IND-type metallo-beta-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.
- Subjects :
- Adult
Amino Acid Sequence
Anti-Bacterial Agents pharmacology
Cefepime
Ceftazidime chemistry
Ceftazidime pharmacology
Cephalexin chemistry
Cephalexin metabolism
Cephalosporins chemistry
Cephalosporins pharmacology
Cephalothin chemistry
Cephalothin metabolism
Chryseobacterium drug effects
Chryseobacterium genetics
Chryseobacterium isolation & purification
Female
Humans
Microbial Sensitivity Tests
Molecular Sequence Data
Phylogeny
Protein Structure, Secondary
Sequence Homology, Amino Acid
beta-Lactamases classification
beta-Lactamases genetics
beta-Lactamases metabolism
Chryseobacterium enzymology
beta-Lactamases chemistry
Subjects
Details
- Language :
- English
- ISSN :
- 1098-6596
- Volume :
- 53
- Issue :
- 10
- Database :
- MEDLINE
- Journal :
- Antimicrobial agents and chemotherapy
- Publication Type :
- Academic Journal
- Accession number :
- 19651915
- Full Text :
- https://doi.org/10.1128/AAC.01607-08