Characterization, cloning and sequence analysis of the inducible Ochrobactrum anthropi AmpC β-lactamase

被引：38

作者：

Higgins, CS ^{[1
]}

Avison, MB ^{[1
]}

Jamieson, L ^{[1
]}

Simm, AM ^{[1
]}

Bennett, PM ^{[1
]}

Walsh, TR ^{[1
]}

机构：

[1] Univ Bristol, Dept Pathol & Microbiol, Sch Med Sci, Bristol Ctr Antimicrobial Res & Evaluat, Bristol BS8 1TD, Avon, England

来源：

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY | 2001年 / 47卷 / 06期

关键词：

D O I：

10.1093/jac/47.6.745

中图分类号：

R51 [传染病];

学科分类号：

100401 ;

摘要：

Ochrobactrum anthropi is resistant to most cephalosporins and penicillins due, at least in part, to the inducible expression of a single beta -lactamase. The beta -lactamase gene has been cloned and sequenced. It encodes an AmpC-type class 1 serine active-site enzyme that hydrolyses mainly cephalosporins and is resistant to inhibition by clavulanic acid. Expression of the ampC gene is inducible via a typical AmpR regulator, which is encoded upstream of ampC. Inducible expression is retained following cloning of O. anthropi ampR-ampC into Escherichia coli, confirming that the signal for AmpR activation in O. anthropi is the same as that used in the Enterobacteriaceae. This is the first reported example of an AmpC beta -ractamase outside of the gamma -subdivision of the bacterial kingdom. Genomic searches of other non-gamma -subdivision bacteria revealed a homologous ampR-ampC cluster in the plant symbiont, Sinorhizobium meliloti.

引用

页码：745 / 754

页数：10

共 31 条

[1] AMINO-ACID SUBSTITUTION OF PROTEINS CODED FOR IN MITOCHONDRIAL-DNA DURING MAMMALIAN EVOLUTION [J].