Molecular characterization of SPM-1, a novel metallo-beta-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme.

The gene encoding the metallo-beta-lactamase SPM-1 was cloned from a genomic library of Pseudomonas aeruginosa strain 48-1997 A. The insert carrying spm-1 possessed a GC content of 47%, indicating that it is of non-Pseudomonas origin. Upstream of spm-1 there is a small open reading frame (ORF), which is homologous to the LysR family of proteins (69% identity to the LysR protein from Salmonella enterica serovar Typhimurium). Downstream of spm-1 there is the start of an ORF, the product of which shows close homology with the GroEL-type proteins from Xanthomonas campestris. No transmissible element could be identified upstream or downstream of spm-1. The spm-1 gene is carried on a plasmid that can transform both Escherichia coli and P. aeruginosa to ceftazidime resistance. SPM-1 contains the classic metallo-beta-lactamase zinc-binding motif HXHXD and shows the highest identity (35.5%) to IMP-1. SPM-1 is a distinctly different metallo-beta-lactamase from VIM and IMP and, accordingly, represents a new subfamily of mobile metallo-beta-lactamases. The predicted molecular weight of the protein was 27 515 Da, significantly higher than that of IMP (25 041 Da) or VIM (25 322 Da). SPM-1 possesses a unique loop of 23 residues that accounts for the higher molecular mass.

[1]  M. Mulvey,et al.  Complete Nucleotide Sequence of a 43-Kilobase Genomic Island Associated with the Multidrug Resistance Region of Salmonella enterica Serovar Typhimurium DT104 and Its Identification in Phage Type DT120 and Serovar Agona , 2001, Journal of bacteriology.

[2]  Timothy R. Walsh,et al.  Sequence analysis of the L1 metallo-β-lactamase from Xanthomonas maltophilia , 1994 .

[3]  S. Gamblin,et al.  Enzyme kinetics and biochemical analysis of ImiS, the metallo-beta-lactamase from Aeromonas sobria 163a. , 1996, The Journal of antimicrobial chemotherapy.

[4]  M. Page.  Understanding metallo β-lactamases , 2002 .

[5]  J. Frère,et al.  Characterization and sequence of the Chryseobacterium (Flavobacterium) meningosepticum carbapenemase: a new molecular class B beta-lactamase showing a broad substrate profile. , 1998, The Biochemical journal.

[6]  Richard A. Moore,et al.  Nosocomial Outbreak of Carbapenem-Resistant Pseudomonas aeruginosa with a New blaIMP Allele, blaIMP-7 , 2002, Antimicrobial Agents and Chemotherapy.

[7]  A P MacGowan,et al.  Sequence analysis and enzyme kinetics of the L2 serine beta-lactamase from Stenotrophomonas maltophilia , 1997, Antimicrobial agents and chemotherapy.

[8]  R. Pridmore.  New and versatile cloning vectors with kanamycin-resistance marker. , 1987, Gene.

[9]  J. Frère,et al.  Purification and Biochemical Characterization of the VIM-1 Metallo-β-Lactamase , 2000, Antimicrobial Agents and Chemotherapy.

[10]  Y. Arakawa,et al.  A novel integron-like element carrying the metallo-beta-lactamase gene blaIMP , 1995, Antimicrobial agents and chemotherapy.

[11]  R M Hall,et al.  Site‐specific insertion of genes into integrons: role of the 59‐base element and determination of the recombination cross‐over point , 1991, Molecular microbiology.

[12]  J. Frère,et al.  Biochemical Characterization of the Pseudomonas aeruginosa 101/1477 Metallo-β-Lactamase IMP-1 Produced byEscherichia coli , 1999, Antimicrobial Agents and Chemotherapy.

[13]  O. Massidda,et al.  The Aeromonas hydrophila cphA gene: molecular heterogeneity among class B metallo-beta-lactamases , 1991, Journal of bacteriology.

[14]  A. Bolmström,et al.  Evaluation of a New Etest for Detecting Metallo-β-Lactamases in Routine Clinical Testing , 2002, Journal of Clinical Microbiology.

[15]  S. Ichiyama,et al.  PCR detection of metallo-beta-lactamase gene (blaIMP) in gram-negative rods resistant to broad-spectrum beta-lactams , 1996, Journal of clinical microbiology.

[16]  N. Woodford,et al.  IMP-4, a Novel Metallo-β-Lactamase from Nosocomial Acinetobacter spp. Collected in Hong Kong between 1994 and 1998 , 2001, Antimicrobial Agents and Chemotherapy.

[17]  G. Cornaglia,et al.  Cloning and Characterization of blaVIM, a New Integron-Borne Metallo-β-Lactamase Gene from a Pseudomonas aeruginosa Clinical Isolate , 1999, Antimicrobial Agents and Chemotherapy.

[18]  M. Hussain,et al.  Cloning and sequencing of the metallothioprotein beta-lactamase II gene of Bacillus cereus 569/H in Escherichia coli , 1985, Journal of bacteriology.

[19]  N. Woodford,et al.  Carbapenemases: a problem in waiting? , 2000, Current opinion in microbiology.

[20]  F. Yoshimura,et al.  Molecular characterization of an enterobacterial metallo beta-lactamase found in a clinical isolate of Serratia marcescens that shows imipenem resistance , 1994, Antimicrobial Agents and Chemotherapy.

[21]  N. Woodford,et al.  Outbreak of Infections Caused by Pseudomonas aeruginosa Producing VIM-1 Carbapenemase in Greece , 2000, Journal of Clinical Microbiology.

[22]  Thierry Naas,et al.  Characterization of VIM-2, a Carbapenem-Hydrolyzing Metallo-β-Lactamase and Its Plasmid- and Integron-Borne Gene from a Pseudomonas aeruginosa Clinical Isolate in France , 2000, Antimicrobial Agents and Chemotherapy.

[23]  A. MacGowan,et al.  Nucleotide and Amino Acid Sequences of the Metallo-β-Lactamase, ImiS, from Aeromonas veronii bv. sobria , 1998, Antimicrobial Agents and Chemotherapy.

[24]  M. Malamy,et al.  Sequencing the gene for an imipenem-cefoxitin-hydrolyzing enzyme (CfiA) from Bacteroides fragilis TAL2480 reveals strong similarity between CfiA and Bacillus cereus beta-lactamase II , 1990, Journal of bacteriology.

[25]  N. Woodford,et al.  Carbapenem-hydrolysing IMP-1 β-lactamase in Klebsiella pneumoniae from Singapore , 1999, The Lancet.

[26]  J. Birnbaum,et al.  MK0787 (N-formimidoyl thienamycin): evaluation of in vitro and in vivo activities , 1980, Antimicrobial Agents and Chemotherapy.

[27]  Y. Arakawa,et al.  Plasmid-mediated dissemination of the metallo-beta-lactamase gene blaIMP among clinically isolated strains of Serratia marcescens , 1995, Antimicrobial agents and chemotherapy.