JAC Advance Access originally published online on October 8, 2002
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Journal of Antimicrobial Chemotherapy (2002) 50, 673-679
© 2002 The British Society for Antimicrobial Chemotherapy
Molecular characterization of SPM-1, a novel metallo-ß-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme
1 Department of Pathology and Microbiology, University of Bristol, Bristol BS8 1TD, UK; 2 Division of Infectious Diseases, Universidade Federal de Sao Paulo, Sao Paulo, Brazil; 3 The JONES Group/JMI Laboratories, North Liberty, IA; 4 Tufts University School of Medicine, Boston, MA, USA
Received 5 July 2002; returned 26 July 2002; revised 20 August 2002; accepted 20 August 2002
The gene encoding the metallo-ß-lactamase SPM-1 was cloned from a genomic library of Pseudomonas aeruginosa strain 48-1997A. 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-ß-lactamase zinc-binding motif HXHXD and shows the highest identity (35.5%) to IMP-1. SPM-1 is a distinctly different metallo-ß-lactamase from VIM and IMP and, accordingly, represents a new subfamily of mobile metallo-ß-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.
Keywords: metallo-ß-lactamase, SENTRY, Pseudomonas aeruginosa
* Corresponding author. Tel: +44-117-928-7522; Fax +44-117-928-7896; E-mail: mark.toleman{at}bristol.ac.uk
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