SHV-27, a novel cefotaxime-hydrolysing β-lactamase, identified in Klebsiella pneumoniae isolates from a Brazilian hospital
SHV-27, a novel cefotaxime-hydrolysing β-lactamase, identified in Klebsiella pneumoniae isolates from a Brazilian hospital
复制标题
DOI：
10.1093/jac/47.4.463
复制
发表时间：
2001-04-01
影响因子：
5.2
通讯作者：
Hart, CA
中科院分区：
文献类型：
--
作者：
Corkill, JE;Cuevas, LE;Hart, CA
从巴西Aracaju一家妇产医院的新生儿血培养标本中分离的头孢噻肟耐药肺炎克雷伯菌中，发现两种分离株（菌株KPBRZ-842和-843，脉冲场凝胶电泳无法区分）分别产生等电点（pl）为5.4和8.2的β-内酰胺酶。使用凝胶覆盖法，头孢噻肟水解被证明是与pI 8.2蛋白。对编码pI 8.2 β-内酰胺酶的基因进行核苷酸测序，发现一个bla（SHV-ESBL）型基因与编码SHV-1的基因有三个沉默点突变，第四个突变导致第156位的氨基酸取代，即天冬氨酸取代甘氨酸。这种新型SHV型超广谱β-内酰胺酶被命名为SHV-27。
From a collection of cefotaxime-resistant Klebsiella pneumoniae isolated from neonatal blood culture specimens in a maternity hospital in Aracaju, Brazil, two isolates (strains KPBRZ-842 and -843, indistinguishable by pulsed-field gel electrophoresis) were found to produce beta -lactamases with isoelectric points (pl) of 5.4 and 8.2, respectively. Using a gel overlay method, cefotaxime hydrolysis was shown to be associated with the pI 8.2 protein. Nucleotide sequencing of the gene encoding the pI 8.2 beta -lactamase revealed a bla(SHV-ESBL)-type gene differing from the gene encoding SHV-1 by three silent point mutations, and a fourth that resulted in an amino acid substitution, aspartate for glycine, at position 156. This novel SHV-type extended-spectrum beta -lactamase is designated SHV-27.