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CMY-4的特性研究,CMY-4是一种在突尼斯奇异变形杆菌临床分离株中发现的AmpC型质粒介导的β-内酰胺酶。

Characterisation of CMY-4, an AmpC-type plasmid-mediated beta-lactamase in a Tunisian clinical isolate of Proteus mirabilis.

作者信息

Verdet C, Arlet G, Ben Redjeb S, Ben Hassen A, Lagrange P H, Philippon A

机构信息

Service de Microbiologie, Université Paris VII Denis Diderot, Hôpital Saint-Louis, France.

出版信息

FEMS Microbiol Lett. 1998 Dec 15;169(2):235-40. doi: 10.1111/j.1574-6968.1998.tb13323.x.

Abstract

A strain of Proteus mirabilis resistant to beta-lactams, including cefoxitin, was isolated from the urine of a woman from Tunisia. Its antibiotic susceptibility pattern and that of the Escherichia coli transconjugant suggested the presence of an AmpC-type beta-lactamase. Two bands of beta-lactamase activity (pI 5.4 and 9.2) were detected by isoelectric focusing. The nucleotide sequence of the gene encoding the AmpC-type enzyme was determined. The deduced amino acid sequence was 98-99% identical to CMY-3 and to those of the plasmid-mediated AmpC-type beta-lactamases originated from Citrobacter freundii and 97% identical to the chromosome-encoded beta-lactamase of a Tunisian clinical isolate of C. freundii. This enzyme differs from CMY-2 by one substitution (Arg for Trp at position 221) and from CMY-3 by two substitutions (Glu for Gly at position 42 and Ser for Asn at position 363) and we propose the denomination CMY-4.

摘要

从一名突尼斯女性尿液中分离出一株对包括头孢西丁在内的β-内酰胺类抗生素耐药的奇异变形杆菌。其抗生素敏感性模式以及大肠杆菌转接合子的敏感性模式表明存在AmpC型β-内酰胺酶。通过等电聚焦检测到两条β-内酰胺酶活性带(pI 5.4和9.2)。测定了编码AmpC型酶的基因的核苷酸序列。推导的氨基酸序列与CMY-3以及源自弗氏柠檬酸杆菌的质粒介导的AmpC型β-内酰胺酶的氨基酸序列有98 - 99%的同一性,与突尼斯弗氏柠檬酸杆菌临床分离株的染色体编码β-内酰胺酶有97%的同一性。该酶与CMY-2在第221位有一个氨基酸替换(色氨酸被精氨酸取代),与CMY-3有两个氨基酸替换(第42位甘氨酸被谷氨酸取代,第363位天冬酰胺被丝氨酸取代),我们提议将其命名为CMY-4。

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