Characterization of a KPC-84 harboring Klebsiella pneumoniae ST11 clinical isolate with ceftazidime-avibactam resistance.

IF 3 3区 医学 Q2 INFECTIOUS DISEASES European Journal of Clinical Microbiology & Infectious Diseases Pub Date : 2024-10-01 Epub Date: 2024-08-07 DOI:10.1007/s10096-024-04910-y
Yanqiao Gong, Yu Feng, Zhiyong Zong, Xiaoju Lv
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Abstract

A novel KPC variant, KPC-84, identified in a Klebsiella pneumoniae isolate from China, exhibits a threonine (T) to proline (P) amino acid substitution at Ambler position 243(T243P), altering from the KPC-2 sequence. Cloning and expression of blaKPC-84 in Escherichia coli, with subsequent MIC assessments, revealed increased resistance to ceftazidime-avibactam and significantly reduced carbapenemase activity compared to KPC-2. Kinetic measurements showed that KPC-84 exhibited sligthly higher hydrolysis of ceftazidime and reduced affinity for avibactam compared to KPC-2. This study emphasizes the emerging diversity of KPC variants with ceftazidime-avibactam resistance, underscoring the complexity of addressing carbapenem-resistant Klebsiella pneumoniae infections.

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具有头孢他啶-阿维菌素耐药性的 KPC-84 型肺炎克雷伯菌 ST11 临床分离株的特征。
在来自中国的肺炎克雷伯氏菌分离物中发现了一种新型 KPC 变体 KPC-84,它在安布勒 243 位(T243P)的苏氨酸(T)到脯氨酸(P)的氨基酸替换,改变了 KPC-2 的序列。blaKPC-84 在大肠杆菌中的克隆和表达以及随后的 MIC 评估表明,与 KPC-2 相比,它对头孢他啶-阿维巴坦的耐药性增强,碳青霉烯酶活性显著降低。动力学测量结果表明,与 KPC-2 相比,KPC-84 对头孢他啶的水解作用略高,对阿维菌素的亲和力降低。这项研究强调了具有头孢他啶-阿维巴坦耐药性的 KPC 变体新出现的多样性,突出了应对耐碳青霉烯类肺炎克雷伯菌感染的复杂性。
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来源期刊
CiteScore
10.40
自引率
2.20%
发文量
138
审稿时长
1 months
期刊介绍: EJCMID is an interdisciplinary journal devoted to the publication of communications on infectious diseases of bacterial, viral and parasitic origin.
期刊最新文献
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