Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives
Abstract IMP-1 metallo-β-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other β-lactam antibiotic...
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| Veröffentlicht in: | FEMS microbiology letters 1999-10, Vol.179 (2), p.289-296 |
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| creator | Hammond, Gail G. Huber, Joann L. Greenlee, Mark L. Laub, Joanne B. Young, Katherine Silver, Lynn L. Balkovec, James M. Pryor, KellyAnn D. Wu, Joseph K. Leiting, Barbara Pompliano, David L. Toney, Jeffrey H. |
| description | Abstract
IMP-1 metallo-β-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other β-lactam antibiotics. A series of thioester derivatives has been shown to competitively inhibit purified IMP-1. As substrates for IMP-1, the thioesters yielded thiol hydrolysis products which themselves were reversible competitive inhibitors. The thioesters also increased sensitivity to the carbapenem L-742,728 in an IMP-1-producing laboratory stain of Escherichia coli, but will need further modification to improve their activity in less permeable organisms such as Pseudomonas and Serratia. Nonetheless, the thioester IMP-1 inhibitors offer an encouraging start to overcoming metallo-β-lactamase-mediated resistance in bacteria. |
| doi_str_mv | 10.1111/j.1574-6968.1999.tb08740.x |
| format | Article |
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IMP-1 metallo-β-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other β-lactam antibiotics. A series of thioester derivatives has been shown to competitively inhibit purified IMP-1. As substrates for IMP-1, the thioesters yielded thiol hydrolysis products which themselves were reversible competitive inhibitors. The thioesters also increased sensitivity to the carbapenem L-742,728 in an IMP-1-producing laboratory stain of Escherichia coli, but will need further modification to improve their activity in less permeable organisms such as Pseudomonas and Serratia. Nonetheless, the thioester IMP-1 inhibitors offer an encouraging start to overcoming metallo-β-lactamase-mediated resistance in bacteria.</description><identifier>ISSN: 0378-1097</identifier><identifier>EISSN: 1574-6968</identifier><identifier>DOI: 10.1111/j.1574-6968.1999.tb08740.x</identifier><language>eng</language><publisher>Oxford, UK: Blackwell Publishing Ltd</publisher><subject>Amides ; Antibiotics ; Bacteria ; Carbapenems ; Clinical isolates ; Derivatives ; E coli ; IMP‐1 ; Inhibitors ; Klebsiella ; Metallo-β-lactamase ; Metallography ; Microbiology ; Pseudomonas aeruginosa ; Sensitivity ; Substrate inhibition ; Thioester ; Thioesters ; β-Lactam antibiotics</subject><ispartof>FEMS microbiology letters, 1999-10, Vol.179 (2), p.289-296</ispartof><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved. 1999</rights><rights>1999 Federation of European Microbiological Societies. Published by Elsevier Science B.V. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1111%2Fj.1574-6968.1999.tb08740.x$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1111%2Fj.1574-6968.1999.tb08740.x$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,776,780,1411,27904,27905,45554,45555</link.rule.ids></links><search><creatorcontrib>Hammond, Gail G.</creatorcontrib><creatorcontrib>Huber, Joann L.</creatorcontrib><creatorcontrib>Greenlee, Mark L.</creatorcontrib><creatorcontrib>Laub, Joanne B.</creatorcontrib><creatorcontrib>Young, Katherine</creatorcontrib><creatorcontrib>Silver, Lynn L.</creatorcontrib><creatorcontrib>Balkovec, James M.</creatorcontrib><creatorcontrib>Pryor, KellyAnn D.</creatorcontrib><creatorcontrib>Wu, Joseph K.</creatorcontrib><creatorcontrib>Leiting, Barbara</creatorcontrib><creatorcontrib>Pompliano, David L.</creatorcontrib><creatorcontrib>Toney, Jeffrey H.</creatorcontrib><title>Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives</title><title>FEMS microbiology letters</title><description>Abstract
IMP-1 metallo-β-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other β-lactam antibiotics. A series of thioester derivatives has been shown to competitively inhibit purified IMP-1. As substrates for IMP-1, the thioesters yielded thiol hydrolysis products which themselves were reversible competitive inhibitors. The thioesters also increased sensitivity to the carbapenem L-742,728 in an IMP-1-producing laboratory stain of Escherichia coli, but will need further modification to improve their activity in less permeable organisms such as Pseudomonas and Serratia. Nonetheless, the thioester IMP-1 inhibitors offer an encouraging start to overcoming metallo-β-lactamase-mediated resistance in bacteria.</description><subject>Amides</subject><subject>Antibiotics</subject><subject>Bacteria</subject><subject>Carbapenems</subject><subject>Clinical isolates</subject><subject>Derivatives</subject><subject>E coli</subject><subject>IMP‐1</subject><subject>Inhibitors</subject><subject>Klebsiella</subject><subject>Metallo-β-lactamase</subject><subject>Metallography</subject><subject>Microbiology</subject><subject>Pseudomonas aeruginosa</subject><subject>Sensitivity</subject><subject>Substrate inhibition</subject><subject>Thioester</subject><subject>Thioesters</subject><subject>β-Lactam 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IMP-1 metallo-β-lactamase is a transferable carbapenem-hydrolyzing enzyme found in some clinical isolates of Pseudomonas aeruginosa, Serratia marcescens and Klebsiella pneumoniae. Bacteria that express IMP-1 show significantly reduced sensitivity to carbapenems and other β-lactam antibiotics. A series of thioester derivatives has been shown to competitively inhibit purified IMP-1. As substrates for IMP-1, the thioesters yielded thiol hydrolysis products which themselves were reversible competitive inhibitors. The thioesters also increased sensitivity to the carbapenem L-742,728 in an IMP-1-producing laboratory stain of Escherichia coli, but will need further modification to improve their activity in less permeable organisms such as Pseudomonas and Serratia. Nonetheless, the thioester IMP-1 inhibitors offer an encouraging start to overcoming metallo-β-lactamase-mediated resistance in bacteria.</abstract><cop>Oxford, UK</cop><pub>Blackwell Publishing Ltd</pub><doi>10.1111/j.1574-6968.1999.tb08740.x</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0378-1097 |
| ispartof | FEMS microbiology letters, 1999-10, Vol.179 (2), p.289-296 |
| issn | 0378-1097 1574-6968 |
| language | eng |
| recordid | cdi_proquest_journals_2311751111 |
| source | Wiley Online Library Journals Frontfile Complete; Oxford University Press Journals All Titles (1996-Current); Alma/SFX Local Collection |
| subjects | Amides Antibiotics Bacteria Carbapenems Clinical isolates Derivatives E coli IMP‐1 Inhibitors Klebsiella Metallo-β-lactamase Metallography Microbiology Pseudomonas aeruginosa Sensitivity Substrate inhibition Thioester Thioesters β-Lactam antibiotics |
| title | Inhibition of IMP-1 metallo-β-lactamase and sensitization of IMP-1-producing bacteria by thioester derivatives |
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