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.
%0 Journal Article
%1 toleman_molecular_2002
%A Toleman, Mark A
%A Simm, Alan M
%A Murphy, Tanya A
%A Gales, Ana C
%A Biedenbach, Doug J
%A Jones, Ronald N
%A Walsh, Timothy R
%D 2002
%J The Journal of Antimicrobial Chemotherapy
%K Acid America, Amino Data, Enzymologic, Expression Gene Humans, Latin Molecular Pseudomonas Regulation, Sequence Sequence, aeruginosa {beta-Lactamases,}
%N 5
%P 673--9
%R 12407123
%T Molecular characterization of SPM-1, a novel metallo-beta-lactamase isolated in Latin America: report from the SENTRY antimicrobial surveillance programme
%U http://www.ncbi.nlm.nih.gov/pubmed/12407123
%V 50
%X 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.
@article{toleman_molecular_2002,
abstract = {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.},
added-at = {2011-03-11T10:05:34.000+0100},
author = {Toleman, Mark A and Simm, Alan M and Murphy, Tanya A and Gales, Ana C and Biedenbach, Doug J and Jones, Ronald N and Walsh, Timothy R},
biburl = {https://www.bibsonomy.org/bibtex/2c1a09bd8278cbf14b928a3a14c2f9267/jelias},
doi = {12407123},
interhash = {3485636de368d033b488a5bc6c27deaf},
intrahash = {c1a09bd8278cbf14b928a3a14c2f9267},
issn = {0305-7453},
journal = {The Journal of Antimicrobial Chemotherapy},
keywords = {Acid America, Amino Data, Enzymologic, Expression Gene Humans, Latin Molecular Pseudomonas Regulation, Sequence Sequence, aeruginosa {beta-Lactamases,}},
month = nov,
note = {{PMID:} 12407123},
number = 5,
pages = {673--9},
shorttitle = {Molecular characterization of {SPM-1,} a novel metallo-beta-lactamase isolated in Latin America},
timestamp = {2011-03-11T10:06:27.000+0100},
title = {Molecular characterization of {SPM-1,} a novel metallo-beta-lactamase isolated in Latin America: report from the {SENTRY} antimicrobial surveillance programme},
url = {http://www.ncbi.nlm.nih.gov/pubmed/12407123},
volume = 50,
year = 2002
}