Clinical and genomic characteristics of IMP-producing Enterobacter cloacae complex and Klebsiella pneumoniae

阴沟肠杆菌 肺炎克雷伯菌 微生物学 肠杆菌科 肠杆菌 克雷伯菌 生物 肠杆菌科感染 病毒学 大肠杆菌 基因 遗传学
作者
Daisuke Suzuki,Aki Sakurai,Mitsutaka Wakuda,Masahiro Suzuki,Yohei Doi
出处
期刊:Antimicrobial Agents and Chemotherapy [American Society for Microbiology]
标识
DOI:10.1128/aac.01672-23
摘要

ABSTRACT Carbapenemase-producing Enterobacterales (CPEs) are one of the top priority antimicrobial-resistant pathogens. Among CPEs, those producing acquired metallo-β-lactamases (MBLs) are considered particularly problematic as few agents are active against them. Imipenemase (IMP) is the most frequently encountered acquired MBL in Japan, but comprehensive assessment of clinical and microbiological features of IMP-producing Enterobacterales infection remains scarce. Here, we retrospectively evaluated 62 patients who were hospitalized at a university hospital in Japan and had IMP-producing Enterobacterales from a clinical culture. The isolates were either Enterobacter cloacae complex or Klebsiella pneumoniae , and most of them were isolated from sputum. The majority of K. pneumoniae, but not E. cloacae complex isolates, were susceptible to aztreonam. Sequence type (ST) 78 and ST517 were prevalent for E. cloacae complex and K. pneumoniae , respectively, and all isolates carried bla IMP-1 . Twenty-four of the patients were deemed infected with IMP-producing Enterobacterales . Among the infected patients, therapy varied and largely consisted of conventional β-lactam agents, fluoroquinolones, or combinations. Three (13%), five (21%), and nine (38%) of them died by days 14, 30, and 90, respectively. While incremental mortality over 90 days was observed in association with underlying comorbidities, active conventional treatment options were available for most patients with IMP-producing Enterobacterales infections, distinguishing them from more multidrug-resistant CPE infections associated with globally common MBLs, such as New Delhi metallo-β-lactamase (NDM) and Verona integron-encoded metallo-β-lactamase (VIM).
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