AAC Accepts, published online ahead of print on 2 November 2009
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Antimicrob. Agents Chemother. doi:10.1128/AAC.01004-09
Copyright (c) 2009, American Society for Microbiology and/or the Listed Authors/Institutions. All Rights Reserved.

Hydrolysis and Inhibition Profiles of {beta}-Lactamases from Molecular Classes A to D with Doripenem, Imipenem and Meropenem

Anne Marie Queenan*, Wenchi Shang, Robert Flamm, and Karen Bush

Johnson & Johnson Pharmaceutical Research and Development, L.L.C., 1000 Route 202 South, Raritan NJ 08869

* To whom correspondence should be addressed. Email: aqueenan{at}its.jnj.com.


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Abstract

Stability of doripenem to hydrolysis by {beta}-lactamases from molecular classes A-D was compared to imipenem and meropenem. Doripenem was stable to hydrolysis by extended-spectrum {beta}-lactamases (ESBLs) and AmpC-type {beta}-lactamases, and demonstrated high affinity for the AmpC enzymes. For the serine carbapenemases, SME-3 and KPC-2, and metallo-{beta}-lactamases, IMP-1 and VIM-2, doripenem hydrolysis was generally 2 to 150-fold slower than imipenem hydrolysis. SPM-1 hydrolyzed meropenem and doripenem four-fold faster than imipenem.






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