Redefining extended-spectrum β-lactamases: balancing science and clinical need
Identifieur interne : 001765 ( Pmc/Curation ); précédent : 001764; suivant : 001766Redefining extended-spectrum β-lactamases: balancing science and clinical need
Auteurs : Christian G. Giske [Suède] ; Arnfinn S. Sundsfjord [Norvège] ; Gunnar Kahlmeter [Suède] ; Neil Woodford [Royaume-Uni] ; Patrice Nordmann [France] ; David L. Paterson [Australie] ; Rafael Cant N [Espagne] ; Timothy R. Walsh [Royaume-Uni]Source :
- Journal of Antimicrobial Chemotherapy [ 0305-7453 ] ; 2008.
Abstract
The current β-lactamase classifications have reached a high level of complexity, making them less accessible to clinicians, infection control professionals, hospital management and politicians. From the clinical perspective, a revised comprehensible nomenclature scheme is therefore needed. The term extended-spectrum β-lactamases (ESBLs) has reached a broader audience over time, but is currently restricted to functional class 2be/molecular class A, clavulanic acid inhibited enzymes with activity against extended-spectrum cephalosporins. The proposed new classification expands the definition of ESBL to other clinically important acquired β-lactamases with activity against extended-spectrum cephalosporins and/or carbapenems. The classical class A ESBLs have been designated ESBLA in this classification, whereas plasmid-mediated AmpC and OXA-ESBLs are classed as miscellaneous ESBLs (ESBLM). Lastly, the carbapenemases have been designated ESBLCARBA, ESBLs with hydrolytic activity against carbapenems. We believe that this simplified classification may encourage new groups of healthcare professionals to engage in the effort to prevent the spread of acquired β-lactamases.
Url:
DOI: 10.1093/jac/dkn444
PubMed: 18957393
PubMed Central: 2721700
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<front><div type="abstract" xml:lang="en"><p>The current β-lactamase classifications have reached a high level of complexity, making them less accessible to clinicians, infection control professionals, hospital management and politicians. From the clinical perspective, a revised comprehensible nomenclature scheme is therefore needed. The term extended-spectrum β-lactamases (ESBLs) has reached a broader audience over time, but is currently restricted to functional class 2be/molecular class A, clavulanic acid inhibited enzymes with activity against extended-spectrum cephalosporins. The proposed new classification expands the definition of ESBL to other clinically important acquired β-lactamases with activity against extended-spectrum cephalosporins and/or carbapenems. The classical class A ESBLs have been designated ESBL<sub>A</sub>
in this classification, whereas plasmid-mediated AmpC and OXA-ESBLs are classed as miscellaneous ESBLs (ESBL<sub>M</sub>
). Lastly, the carbapenemases have been designated ESBL<sub>CARBA</sub>
, ESBLs with hydrolytic activity against carbapenems. We believe that this simplified classification may encourage new groups of healthcare professionals to engage in the effort to prevent the spread of acquired β-lactamases.</p>
</div>
</front>
</TEI>
<pmc article-type="research-article"><pmc-comment>The publisher of this article does not allow downloading of the full text in XML form.</pmc-comment>
<front><journal-meta><journal-id journal-id-type="nlm-ta">J Antimicrob Chemother</journal-id>
<journal-id journal-id-type="publisher-id">jac</journal-id>
<journal-id journal-id-type="hwp">jac</journal-id>
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<article-id pub-id-type="publisher-id">dkn444</article-id>
<article-categories><subj-group subj-group-type="heading"><subject>Leading Articles</subject>
</subj-group>
</article-categories>
<title-group><article-title>Redefining extended-spectrum β-lactamases: balancing science and clinical need</article-title>
</title-group>
<contrib-group><contrib contrib-type="author"><name><surname>Giske</surname>
<given-names>Christian G.</given-names>
</name>
<xref ref-type="aff" rid="af1">1</xref>
<xref ref-type="corresp" rid="cor1">*</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Sundsfjord</surname>
<given-names>Arnfinn S.</given-names>
</name>
<xref ref-type="aff" rid="af2">2</xref>
<xref ref-type="aff" rid="af3">3</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Kahlmeter</surname>
<given-names>Gunnar</given-names>
</name>
<xref ref-type="aff" rid="af4">4</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Woodford</surname>
<given-names>Neil</given-names>
</name>
<xref ref-type="aff" rid="af5">5</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Nordmann</surname>
<given-names>Patrice</given-names>
</name>
<xref ref-type="aff" rid="af6">6</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Paterson</surname>
<given-names>David L.</given-names>
</name>
<xref ref-type="aff" rid="af7">7</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Cantón</surname>
<given-names>Rafael</given-names>
</name>
<xref ref-type="aff" rid="af8">8</xref>
</contrib>
<contrib contrib-type="author"><name><surname>Walsh</surname>
<given-names>Timothy R.</given-names>
</name>
<xref ref-type="aff" rid="af9">9</xref>
</contrib>
</contrib-group>
<aff id="af1"><label>1</label>
<addr-line>Clinical Microbiology</addr-line>
,<institution>Karolinska University Hospital</institution>
,<addr-line>Stockholm</addr-line>
,<country>Sweden</country>
</aff>
<aff id="af2"><label>2</label>
<addr-line>Department of Microbiology and Infection Control</addr-line>
,<institution>University Hospital of Northern Norway</institution>
,<country>Norway</country>
</aff>
<aff id="af3"><label>3</label>
<addr-line>Section for Microbiology and Virology, Department of Medical Biology</addr-line>
,<institution>University of Tromsø</institution>
,<addr-line>Tromsø</addr-line>
,<country>Norway</country>
</aff>
<aff id="af4"><label>4</label>
<addr-line>Department of Clinical Microbiology</addr-line>
,<institution>Central Hospital</institution>
,<addr-line>Växjö</addr-line>
,<country>Sweden</country>
</aff>
<aff id="af5"><label>5</label>
<addr-line>Antibiotic Resistance Monitoring and Reference Laboratory</addr-line>
,<institution>Centre for Infections, Health Protection Agency</institution>
,<addr-line>London</addr-line>
,<country>UK</country>
</aff>
<aff id="af6"><label>6</label>
<addr-line>Service de Bactériologie-Virologie</addr-line>
,<institution>Hôpital de Bicêtre, Assistance Publique-Hôpitaux de Paris, Faculté de Médecine, Université Paris-Sud</institution>
,<country>France</country>
</aff>
<aff id="af7"><label>7</label>
<institution>University of Queensland Centre for Clinical Research and Royal Brisbane and Women's Hospital</institution>
,<addr-line>Brisbane</addr-line>
,<country>Australia</country>
</aff>
<aff id="af8"><label>8</label>
<addr-line>Servicio de Microbiología</addr-line>
,<institution>Hospital Universitario Ramón y Cajal</institution>
,<addr-line>Madrid</addr-line>
,<country>Spain</country>
</aff>
<aff id="af9"><label>9</label>
<addr-line>School of Medicine</addr-line>
,<institution>Cardiff University</institution>
,<addr-line>Cardiff, Wales</addr-line>
,<country>UK</country>
</aff>
<author-notes><corresp id="cor1"><label>*</label>
Corresponding author. Tel: <phone>+46-8-517-73574</phone>
; Fax: <fax>+46-8-30-8099</fax>
; E-mail: <email>christian.giske@karolinska.se</email>
</corresp>
</author-notes>
<pub-date pub-type="ppub"><month>1</month>
<year>2009</year>
</pub-date>
<pub-date pub-type="epub"><day>28</day>
<month>10</month>
<year>2008</year>
</pub-date>
<volume>63</volume>
<issue>1</issue>
<fpage>1</fpage>
<lpage>4</lpage>
<permissions><copyright-statement>© The Author 2008. Published by Oxford University Press on behalf of the British Society for Antimicrobial Chemotherapy. All rights reserved. For Permissions, please e-mail: journals.permissions@oxfordjournals.org</copyright-statement>
</permissions>
<abstract><p>The current β-lactamase classifications have reached a high level of complexity, making them less accessible to clinicians, infection control professionals, hospital management and politicians. From the clinical perspective, a revised comprehensible nomenclature scheme is therefore needed. The term extended-spectrum β-lactamases (ESBLs) has reached a broader audience over time, but is currently restricted to functional class 2be/molecular class A, clavulanic acid inhibited enzymes with activity against extended-spectrum cephalosporins. The proposed new classification expands the definition of ESBL to other clinically important acquired β-lactamases with activity against extended-spectrum cephalosporins and/or carbapenems. The classical class A ESBLs have been designated ESBL<sub>A</sub>
in this classification, whereas plasmid-mediated AmpC and OXA-ESBLs are classed as miscellaneous ESBLs (ESBL<sub>M</sub>
). Lastly, the carbapenemases have been designated ESBL<sub>CARBA</sub>
, ESBLs with hydrolytic activity against carbapenems. We believe that this simplified classification may encourage new groups of healthcare professionals to engage in the effort to prevent the spread of acquired β-lactamases.</p>
</abstract>
<kwd-group><title>Keywords</title>
<kwd>classification</kwd>
<kwd>ESBLs</kwd>
<kwd>metallo-β-lactamases</kwd>
<kwd>OXA</kwd>
<kwd>KPC</kwd>
</kwd-group>
</article-meta>
</front>
</pmc>
</record>
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