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Mechanisms of Resistance

SME-Type Carbapenem-Hydrolyzing Class A β-Lactamases from Geographically Diverse Serratia marcescens Strains

Anne Marie Queenan, Carlos Torres-Viera, Howard S. Gold, Yehuda Carmeli, George M. Eliopoulos, Robert C. Moellering Jr., John P. Quinn, Janet Hindler, Antone A. Medeiros, Karen Bush
Anne Marie Queenan
The R. W. Johnson Pharmaceutical Research Institute, Raritan, New Jersey 08869;
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Carlos Torres-Viera
Beth Israel Deaconess Medical Center and
Harvard Medical School, Boston, Massachusetts 02115;
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Howard S. Gold
Beth Israel Deaconess Medical Center and
Harvard Medical School, Boston, Massachusetts 02115;
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Yehuda Carmeli
Beth Israel Deaconess Medical Center and
Harvard Medical School, Boston, Massachusetts 02115;
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George M. Eliopoulos
Beth Israel Deaconess Medical Center and
Harvard Medical School, Boston, Massachusetts 02115;
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Robert C. Moellering Jr.
Beth Israel Deaconess Medical Center and
Harvard Medical School, Boston, Massachusetts 02115;
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John P. Quinn
University of Illinois, Chicago, Illinois 60614;
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Janet Hindler
University of California at Los Angeles Medical Center, Los Angeles, California 90024; and
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Antone A. Medeiros
Miriam Hospital, Brown University, Providence, Rhode Island 02906
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Karen Bush
The R. W. Johnson Pharmaceutical Research Institute, Raritan, New Jersey 08869;
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DOI: 10.1128/AAC.44.11.3035-3039.2000
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ABSTRACT

Three sets of carbapenem-resistant Serratia marcescensisolates have been identified in the United States: 1 isolate in Minnesota in 1985 (before approval of carbapenems for clinical use), 5 isolates in Los Angeles (University of California at Los Angeles [UCLA]) in 1992, and 19 isolates in Boston from 1994 to 1999. All isolates tested produced two β-lactamases, an AmpC-type enzyme with pI values of 8.6 to 9.0 and one with a pI value of approximately 9.5. The enzyme with the higher pI in each strain hydrolyzed carbapenems and was not inhibited by EDTA, similar to the chromosomal class A SME-1 β-lactamase isolated from the 1982 London strain S. marcescens S6. The genes encoding the carbapenem-hydrolyzing enzymes were cloned in Escherichia coli and sequenced. The enzyme from the Minnesota isolate had an amino acid sequence identical to that of SME-1. The isolates from Boston and UCLA produced SME-2, an enzyme with a single amino acid change relative to SME-1, a substitution from valine to glutamine at position 207. Purified SME enzymes from the U.S. isolates had β-lactam hydrolysis profiles similar to that of the London SME-1 enzyme. Pulsed-field gel electrophoresis analysis revealed that the isolates showed some similarity but differed by at least three genetic events. In conclusion, a family of rare class A carbapenem-hydrolyzing β-lactamases first described in London has now been identified inS. marcescens isolates across the United States.

  • Copyright © 2000 American Society for Microbiology
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SME-Type Carbapenem-Hydrolyzing Class A β-Lactamases from Geographically Diverse Serratia marcescens Strains
Anne Marie Queenan, Carlos Torres-Viera, Howard S. Gold, Yehuda Carmeli, George M. Eliopoulos, Robert C. Moellering Jr., John P. Quinn, Janet Hindler, Antone A. Medeiros, Karen Bush
Antimicrobial Agents and Chemotherapy Nov 2000, 44 (11) 3035-3039; DOI: 10.1128/AAC.44.11.3035-3039.2000

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SME-Type Carbapenem-Hydrolyzing Class A β-Lactamases from Geographically Diverse Serratia marcescens Strains
Anne Marie Queenan, Carlos Torres-Viera, Howard S. Gold, Yehuda Carmeli, George M. Eliopoulos, Robert C. Moellering Jr., John P. Quinn, Janet Hindler, Antone A. Medeiros, Karen Bush
Antimicrobial Agents and Chemotherapy Nov 2000, 44 (11) 3035-3039; DOI: 10.1128/AAC.44.11.3035-3039.2000
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KEYWORDS

carbapenems
Serratia marcescens
beta-lactamases

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