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肠杆菌科碳青霉烯水解酶 OXA-232 的遗传和生化特性研究。

Genetic and biochemical characterisation of OXA-232, a carbapenem-hydrolysing class D β-lactamase from Enterobacteriaceae.

机构信息

Service de Bactériologie-Virologie, INSERM U914 Emerging Resistance to Antibiotics, Hôpital de Bicêtre, Assistance Publique/Hôpitaux de Paris, Faculté de Médecine et Université Paris-Sud, K. Bicêtre, France.

出版信息

Int J Antimicrob Agents. 2013 Apr;41(4):325-9. doi: 10.1016/j.ijantimicag.2012.11.007. Epub 2013 Jan 8.

DOI:10.1016/j.ijantimicag.2012.11.007
PMID:23305656
Abstract

Three enterobacterial isolates (two Klebsiella pneumoniae and one Escherichia coli) were recovered from three patients transferred from India to France in 2011. All three isolates were resistant or of intermediate susceptibility to all β-lactams and of decreased susceptibility to carbapenems. These three isolates expressed a novel carbapenem-hydrolysing β-lactamase, OXA-232, differing from OXA-181 and OXA-48 by one and five amino acid substitutions, respectively. Compared with OXA-181, OXA-232 had a lower ability to hydrolyse carbapenems but conversely possessed higher hydrolytic activities against penicillins. The bla(OXA-232) gene was located on a 6.1-kb ColE-type non-conjugative plasmid.

摘要

2011 年,从印度转往法国的 3 名患者身上分离出 3 株肠杆菌(2 株肺炎克雷伯菌和 1 株大肠埃希菌)。这 3 株分离株均对所有β-内酰胺类药物表现出耐药性或中介敏感性,对碳青霉烯类药物的敏感性降低。这 3 株分离株均表达一种新型碳青霉烯水解β-内酰胺酶,OXA-232,与 OXA-181 和 OXA-48 分别有 1 个和 5 个氨基酸取代。与 OXA-181 相比,OXA-232 对碳青霉烯类药物的水解能力较低,但对青霉素的水解活性却较高。bla(OXA-232)基因位于一个 6.1kb 的 ColE 型非接合性质粒上。

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