Extended-spectrum β-lactamase controversies

摘要：

@@ What is an ESBL?What seemed like a simple concept when the name ESBL was introduced has become more complicated as more enzymes with related properties have been recognized. The first enzymes to be termed extended-spectrum β-lactamases (ESBLs) were found to differ from the common, plasmid-mediated, broadspectrum SHV-1, TEM-1, or TEM-2 β-lactamases by a small number of amino acid substitutions located near the active site that modified its structure so as to extend the spectrum of the parental enzyme”1-3”. Later ESBLs related to OXA-2 or OXA-10 were discovered that also differed from their progenitors by a limited number of amino acid substitutions”4-5”. These enzymes conferred resistance to oxyirnino-β-lactams such as cefotaxime, ceftazidime, ceftriaxone, and aztreonam and were at least as susceptible to β-lactamase inhibitors (clavulanic acid or sulbactam) as the parental types (with the OXA enzymes notably less susceptible than those in the TEM or SHV families)”6”.

机标关键词：amino acid、active site

所属期刊栏目：6

分类号：R3(基础医学)

在线出版日期：2007-01-22（万方平台首次上网日期，不代表论文的发表时间）

页数：共10页

页码：361-370