Molecular characterization of a carbapenem-hydrolyzing β-lactamase from Chryseobacterium ( Flavobacterium) indologenes

Chryseobacterium ( Flavobacterium) indologenes 001 clinical strain was resistant to several β-lactam classes including carbapenems. Shotgun cloning experiments of Sau3AI restricted genomic DNA of C. indologenes 001 into pBKCMV cloning vector followed by transformation into Escherichia coli DH10B gav...

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Veröffentlicht in:	FEMS microbiology letters 1999-02, Vol.171 (2), p.127-132
Hauptverfasser:	Bellais, Samuel, Léotard, Sophie, Poirel, Laurent, Naas, Thierry, Nordmann, Patrice
Format:	Artikel
Sprache:	eng
Schlagworte:	Antibacterial agents Antibiotics. Antiinfectious agents. Antiparasitic agents Bacteriology Base Sequence beta-Lactam Resistance - genetics beta-Lactamases - genetics beta-Lactamases - metabolism Biological and medical sciences Carbapenemase Carbapenems - metabolism Carbapenems - pharmacology Chryseobacterium ( Flavobacterium) indologenes Cloning, Molecular Flavobacterium - drug effects Flavobacterium - enzymology Flavobacterium - genetics Fundamental and applied biological sciences. Psychology Gene Expression Regulation, Bacterial - drug effects Genes, Bacterial - drug effects Genetics Kinetics Medical sciences Metallo-β-lactamase Microbial Sensitivity Tests Microbiology Molecular Sequence Data Pharmacology. Drug treatments Plasmids Recombinant Proteins Restriction Mapping Sequence Homology, Amino Acid Substrate Specificity Transformation, Genetic β-Lactamase
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Zusammenfassung:	Chryseobacterium ( Flavobacterium) indologenes 001 clinical strain was resistant to several β-lactam classes including carbapenems. Shotgun cloning experiments of Sau3AI restricted genomic DNA of C. indologenes 001 into pBKCMV cloning vector followed by transformation into Escherichia coli DH10B gave one recombinant plasmid possessing a 4.2-kb DNA insert. It encoded a p I 7.2 β-lactamase of 239 amino acids (IND-1) which is a metallo-enzyme with a broad spectrum β-lactam hydrolysis profile. This class B carbapenem-hydrolyzing β-lactamase shares the highest identity (43%) with BlaB from C. meningosepticum, thus showing heterogeneity of carbapenem-hydrolyzing β-lactamases in Chryseobacterium spp.
ISSN:	0378-1097 1574-6968
DOI:	10.1016/S0378-1097(98)00594-1