Vuye A, Verschraegen G, Claeys G
Department of Pharmaceutical Microbiology, University of Ghent, Belgium.
Antimicrob Agents Chemother. 1989 May;33(5):757-61. doi: 10.1128/AAC.33.5.757.
Low-level transferable resistance to ceftazidime was detected in seven strains of Klebsiella pneumoniae and one strain of Escherichia coli. Six of the Klebsiella strains and the E. coli strain were shown to produce a novel beta-lactamase (CAZ-lo) with a pI of 5.6 that hydrolyzed broad-spectrum cephalosporins at low but comparable levels. One strain of K. pneumoniae was of a serotype different from that of the other strains and produced a plasmid-encoded cefuroximase (FUR) with a pI of 7.5 that mediated moderate levels of resistance to different broad-spectrum cephalosporins. High-level resistance to ceftazidime was detected in one other strain of K. pneumoniae, which produced a beta-lactamase with a pI of 6.5 (CAZ-hi). Apart from its pI, this enzyme differed from CAZ-lo by a specific and high hydrolytic activity against ceftazidime. The epidemiological context suggested that CAZ-hi may be a mutant of CAZ-lo, and this hypothesis was supported by the isolation of laboratory mutants of CAZ-lo showing properties identical to those of the clinical CAZ-hi enzyme.
在7株肺炎克雷伯菌和1株大肠杆菌中检测到对头孢他啶的低水平可转移耐药性。其中6株肺炎克雷伯菌和该株大肠杆菌产生了一种新型β-内酰胺酶(CAZ-lo),其pI为5.6,能在较低但相当的水平水解广谱头孢菌素。1株肺炎克雷伯菌的血清型与其他菌株不同,产生了一种质粒编码的头孢呋辛酶(FUR),其pI为7.5,介导对不同广谱头孢菌素的中度耐药性。在另一株肺炎克雷伯菌中检测到对头孢他啶的高水平耐药性,该菌株产生了一种pI为6.5的β-内酰胺酶(CAZ-hi)。除了其pI外,这种酶与CAZ-lo的不同之处在于对头孢他啶具有特异性的高水解活性。流行病学背景表明,CAZ-hi可能是CAZ-lo的突变体,这一假设得到了实验室分离出的与临床CAZ-hi酶特性相同的CAZ-lo突变体的支持。