在体内或体外筛选出的新型源自OXA-10的超广谱β-内酰胺酶。
Novel OXA-10-derived extended-spectrum beta-lactamases selected in vivo or in vitro.
作者信息
Mugnier P, Casin I, Bouthors A T, Collatz E
机构信息
Laboratoire de Recherche Moléculaire sur les Antibiotiques, UFR Broussais-Hôtel Dieu and UFR Pitié-Salpêtrière, Université Paris VI.
出版信息
Antimicrob Agents Chemother. 1998 Dec;42(12):3113-6. doi: 10.1128/AAC.42.12.3113.
Abstract
A clinical isolate of Pseudomonas aeruginosa, PAe191, was found to be highly resistant to all anti-Pseudomonas beta-lactam antibiotics (except imipenem) and resistant also to aminoglycosides. It produced a beta-lactamase (with an apparent pI of 7.6) which was not inhibited by clavulanic acid. Cloning and characterization of the beta-lactamase gene showed that it coded for a novel extended-spectrum OXA-10 variant, called OXA-19, which differed from OXA-10 by nine amino acids and from OXA-13 by two, i.e., Asn in position 73 (Asn73) instead of Ser and Asp157 instead of Gly. Asparagine in position 157 is implicated in resistance to ceftazidime, while the amino acid in position 73, in this variant, seems to condition the level of resistance to penicillins. The oxa19 gene was found to be inserted, in a typical integron structure, immediately downstream from an aac(6')-Ib gene coding for an aminoglycoside acetyltransferase variant, which was called AAC(6')-Ib9.
摘要
一株铜绿假单胞菌临床分离株PAe191，被发现对所有抗假单胞菌β-内酰胺类抗生素（亚胺培南除外）高度耐药，并且对氨基糖苷类也耐药。它产生一种β-内酰胺酶（表观pI为7.6），克拉维酸对其无抑制作用。β-内酰胺酶基因的克隆和特性分析表明，它编码一种新型的超广谱OXA-10变体，称为OXA-19，它与OXA-10有9个氨基酸不同，与OXA-13有2个氨基酸不同，即第73位的天冬酰胺（Asn73）取代了丝氨酸，第157位的天冬氨酸取代了甘氨酸。第157位的天冬酰胺与对头孢他啶的耐药性有关，而在这个变体中，第73位的氨基酸似乎决定了对青霉素的耐药水平。发现oxa19基因以典型的整合子结构插入到编码一种氨基糖苷类乙酰转移酶变体（称为AAC(6')-Ib9）的aac(6')-Ib基因的紧邻下游。
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