rdf:type |
|
lifeskim:mentions |
|
pubmed:issue |
7
|
pubmed:dateCreated |
2009-6-25
|
pubmed:databankReference |
|
pubmed:abstractText |
Acinetobacter baumannii isolate KAR was uncommonly more resistant to cefepime and cefpirome than to ceftazidime and cefotaxime. Cloning and expression of the beta-lactamase gene content of this isolate into Escherichia coli TOP10 identified ss-lactamase RTG-4 (or CARB-10), which corresponds to the first reported extended-spectrum CARB-type enzyme. RTG-4 is a plasmid-encoded Ambler class A beta-lactamase whose sequence differs by 4 amino acid substitutions from the narrow-spectrum beta-lactamase RTG-3. RTG-4 hydrolyzes cefepime and cefpirome and weakly hydrolyzes ceftazidime due to the single Ser-to-Thr substitution at Ambler position 69. RTG-4 is less susceptible to inhibition by tazobactam and sulbactam than RTG-3. Expression of beta-lactamase RTG-4 in a wild-type A. baumannii reference strain showed that it conferred resistance to cefepime and cefpirome. The genetic environment of the bla(RTG-4) gene was made of a peculiar transposon located on a ca. 50-kb plasmid. ISAba9, located upstream of bla(RTG-4), may be responsible for its acquisition by recognizing a secondary right inverted repeat sequence, thus acting by a one-ended transposition process.
|
pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-10049269,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-10223920,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-10350372,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-10722515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-11158739,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-11959558,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-12069969,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-12709319,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-12936998,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-15388476,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-15616333,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-16048925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-1650733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-16882287,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-16894514,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-16894515,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-17050816,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-18154527,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-1840585,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-18519717,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-2039479,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-3087285,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-3128280,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-385575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-6276367,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-6327987,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-6387733,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-8341713,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-8964033,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-9281821,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-9333046,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-9687391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-9729608,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19380596-9925522
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
|
pubmed:status |
MEDLINE
|
pubmed:month |
Jul
|
pubmed:issn |
1098-6596
|
pubmed:author |
|
pubmed:issnType |
Electronic
|
pubmed:volume |
53
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3010-6
|
pubmed:dateRevised |
2010-9-27
|
pubmed:meshHeading |
pubmed-meshheading:19380596-Acinetobacter baumannii,
pubmed-meshheading:19380596-Amino Acid Sequence,
pubmed-meshheading:19380596-Anti-Bacterial Agents,
pubmed-meshheading:19380596-Drug Resistance, Bacterial,
pubmed-meshheading:19380596-Escherichia coli,
pubmed-meshheading:19380596-Kinetics,
pubmed-meshheading:19380596-Microbial Sensitivity Tests,
pubmed-meshheading:19380596-Molecular Sequence Data,
pubmed-meshheading:19380596-Mutagenesis, Site-Directed,
pubmed-meshheading:19380596-beta-Lactamases
|
pubmed:year |
2009
|
pubmed:articleTitle |
Genetic and biochemical characterization of the first extended-spectrum CARB-type beta-lactamase, RTG-4, from Acinetobacter baumannii.
|
pubmed:affiliation |
Service de Bactériologie-Virologie-Hygiène, Hôpital de Bicêtre, Faculté de Médecine et Université Paris-Sud, 78 rue de Général Leclerc, Le Kremlin-Bicêtre Cedex 94275, France.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|