Molecular characterization of chromosomal class C β-lactamase and its regulatory gene in Ochrobactrum anthropi
Molecular characterization of chromosomal class C β-lactamase and its regulatory gene in Ochrobactrum anthropi
复制标题
DOI:
10.1128/aac.45.8.2324-2330.2001
复制
发表时间:
2001-08-01
影响因子:
4.9
通讯作者:
Arlet, G
中科院分区:
文献类型:
--
作者:
Nadjar, D;Labia, R;Arlet, G
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 mug/ml and of cefepime were 64 to > 128 mug/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. amthropi 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 mug/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 mere 96 to 99% identical to the sequence of the clinical strain. The beta -lactamase characterized from strain SLO74 nas named OCH-1 (gene, bla(OCH-I)).