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鲍曼不动杆菌天然存在的苯唑西林酶的特性研究。

Characterization of the naturally occurring oxacillinase of Acinetobacter baumannii.

作者信息

Héritier Claire, Poirel Laurent, Fournier Pierre-Edouard, Claverie Jean-Michel, Raoult Didier, Nordmann Patrice

机构信息

Service de Bactériologie-Virologie, Hôpital de Bicêtre, Le Kremlin-Bicêtre, France.

出版信息

Antimicrob Agents Chemother. 2005 Oct;49(10):4174-9. doi: 10.1128/AAC.49.10.4174-4179.2005.

Abstract

A chromosomally encoded oxacillinase, OXA-69, was characterized from Acinetobacter baumannii AYE. beta-Lactamase OXA-69 shared 97% amino acid identity with the recently described OXA-51 enzyme of A. baumannii and 62 and 56% amino acid identity with the carbapenem-hydrolyzing oxacillinases OXA-24 and OXA-23, respectively. Biochemical characterization of the purified OXA-69 revealed a narrow-spectrum hydrolysis profile but including, at a low level, imipenem and meropenem. By PCR and sequencing bla(OXA-69)-like genes were identified in all A. baumannii strains tested (n = 12), suggesting that this oxacillinase is naturally occurring in that species.

摘要

从鲍曼不动杆菌AYE中鉴定出一种染色体编码的苯唑西林酶OXA-69。β-内酰胺酶OXA-69与最近描述的鲍曼不动杆菌OXA-51酶具有97%的氨基酸同一性,与碳青霉烯水解苯唑西林酶OXA-24和OXA-23分别具有62%和56%的氨基酸同一性。纯化的OXA-69的生化特性显示出窄谱水解谱,但包括低水平的亚胺培南和美罗培南。通过PCR和测序,在所有测试的鲍曼不动杆菌菌株(n = 12)中鉴定出bla(OXA-69)样基因,表明该苯唑西林酶在该菌种中天然存在。

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