Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2001-7-13
pubmed:abstractText
Ochrobactrum anthropi, formerly known as CDC group Vd, is an oxidase-producing, gram-negative, obligately aerobic, non-lactose-fermenting bacillus of low virulence that occasionally causes human infections. It is highly resistant to all beta-lactams except imipenem. A clinical isolate, SLO74, and six reference strains were tested. MICs of penicillins, aztreonam, and most cephalosporins tested, including cefotaxime and ceftazidime, were >128 microg/ml and of cefepime were 64 to >128 microg/ml. Clavulanic acid was ineffective and tazobactam had a weak effect in association with piperacillin. Two genes, ampR and ampC, were cloned by inserting restriction fragments of genomic DNA from the clinical strain O. anthropi SLO74 into pBK-CMV to give the recombinant plasmid pBK-OA1. The pattern of resistance to beta-lactams of this clone was similar to that of the parental strain, except for its resistance to cefepime (MIC, 0.5 ,micro/ml). The deduced amino acid sequence of the AmpC beta-lactamase (pI, 8.9) was only 41 to 52% identical to the sequence of other chromosomally encoded and plasmid-encoded class C beta-lactamases. The kinetic properties of this beta-lactamase were typical for this class of beta-lactamases. Upstream from the ampC gene, the ampR gene encodes a protein with a sequence that is 46 to 62% identical to those of other AmpR proteins and with an amino-terminal DNA-binding domain typical of transcriptional activators of the Lys-R family. The deduced amino acid sequences of the ampC genes of the six reference strains were 96 to 99% identical to the sequence of the clinical strain. The beta-lactamase characterized from strain SLO74 was named OCH-1 (gene, bla(OCH-I)).
pubmed:commentsCorrections
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pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0066-4804
pubmed:author
pubmed:issnType
Print
pubmed:volume
45
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2324-30
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:11451692-Amino Acid Sequence, pubmed-meshheading:11451692-Anti-Bacterial Agents, pubmed-meshheading:11451692-Bacterial Proteins, pubmed-meshheading:11451692-Base Sequence, pubmed-meshheading:11451692-Chromosomes, pubmed-meshheading:11451692-Chromosomes, Bacterial, pubmed-meshheading:11451692-DNA Primers, pubmed-meshheading:11451692-Drug Resistance, Multiple, pubmed-meshheading:11451692-Isoelectric Focusing, pubmed-meshheading:11451692-Microbial Sensitivity Tests, pubmed-meshheading:11451692-Molecular Sequence Data, pubmed-meshheading:11451692-Ochrobactrum anthropi, pubmed-meshheading:11451692-Phylogeny, pubmed-meshheading:11451692-Polymerase Chain Reaction, pubmed-meshheading:11451692-Sequence Homology, Amino Acid, pubmed-meshheading:11451692-beta-Lactamases, pubmed-meshheading:11451692-beta-Lactams
pubmed:year
2001
pubmed:articleTitle
Molecular characterization of chromosomal class C beta-lactamase and its regulatory gene in Ochrobactrum anthropi.
pubmed:affiliation
Laboratoire de Bactériologie, Hôpital Tenon, UFR Saint-Antoine, Paris, France.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't