Dataset Information

Sfh-I, a subclass B2 metallo-beta-lactamase from a Serratia fonticola environmental isolate.

ABSTRACT: An environmental isolate of Serratia fonticola resistant to carbapenems was shown to contain a genetic determinant encoding a metallo-beta-lactamase of the subclass B2. The Sfh-I enzyme exhibits some divergence from the previously characterized enzymes of this subclass. This is the first example of a naturally occurring metallo-beta-lactamase in Enterobacteriaceae.

SUBMITTER: Saavedra MJ

PROVIDER: S-EPMC161872 | biostudies-literature | 2003 Jul

REPOSITORIES: biostudies-literature

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Sfh-I, a subclass B2 metallo-beta-lactamase from a Serratia fonticola environmental isolate.

Saavedra Maria José MJ Peixe Luísa L Sousa João Carlos JC Henriques Isabel I Alves Artur A Correia António A

Antimicrobial agents and chemotherapy 20030701 7

An environmental isolate of Serratia fonticola resistant to carbapenems was shown to contain a genetic determinant encoding a metallo-beta-lactamase of the subclass B2. The Sfh-I enzyme exhibits some divergence from the previously characterized enzymes of this subclass. This is the first example of a naturally occurring metallo-beta-lactamase in Enterobacteriaceae. ...[more]

PMID: 12821491

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Project description:A clinical isolate of Serratia marcescens (TN9106) produced a metallo beta-lactamase (IMP-1) which conferred resistance to imipenem and broad-spectrum beta-lactams. The blaIMP gene providing imipenem resistance was cloned and expressed in Escherichia coli HB101. The IMP-1 was purified from E. coli HB101 that harbors pSMBNU24 carrying blaIMP, and its apparent molecular mass was calculated to be about 30 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Kinetic studies of IMP-1 against various beta-lactams revealed that this enzyme hydrolyzes not only various broad-spectrum beta-lactams but also carbapenems. However, aztreonam was relatively stable against IMP-1. Although clavulanate or cloxacillin failed to inhibit IMP-1, Hg2+, Fe2+, or Cu2+ blocked the enzyme's activity. Moreover, the presence of EDTA in the reaction buffer resulted in a decrease in the enzyme's activity. Carbapenem resistance was not transferred from S. marcescens TN9106 to E. coli CSH2 by conjugation. A hybridization study confirmed that blaIMP was encoded on the chromosome of S. marcescens TN9106. By nucleotide sequencing analysis, blaIMP was found to encode a protein of 246 amino acid residues and was shown to have considerable homology to the metallo beta-lactamase genes of Bacillus cereus, Bacteroides fragilis, and Aeromonas hydrophila. The G+C content of blaIMP was 39.4%. Four consensus amino acid residues, His-95, His-97, Cys-176, and His-215, which form putative zinc ligands, were conserved in the deduced amino acid sequence of IMP-1. By determination of the amino acid sequence at the N terminus of purified mature IMP-1, 18 amino acid residues were found to be processed from the N terminus of the premature enzyme as a signal peptide. These results clearly show that IMP-1 is an enterobacterial metallo beta-lactamase, of which the primary structure has been completely determined, that confers resistance to carbapenems and other broad-spectrum beta-lactams.

Dataset Information

Sfh-I, a subclass B2 metallo-beta-lactamase from a Serratia fonticola environmental isolate.

Publications

Sfh-I, a subclass B2 metallo-beta-lactamase from a Serratia fonticola environmental isolate.

Similar Datasets

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