INTRODUCTION Expanded-spectrum cephalosporins are b-lactams with a broad spectrum of activity against most Gram-negative bacteria [1]. However, they are sensitive to hydrolysis by several b-lactamases, including extended-spectrum b-lactamases (ES- BLs). Most ESBLs belong to class A of the Ambler nomenclature [2], possessing an active site serine and being mostly susceptible to inhibition by clavulanic acid. The genes encoding these ac- quired b-lactamases are mostly plasmid-mediated and are increasingly reported.The most common ESBLs identified in the past were those of the TEM and SHV types, which evolved via mutation of earlier penicillinases. The SHV-type ESBLs were considered, until recently, to be the most frequent ESBLs, although TEM ESBLs are also extremely common [1]. Other ESBLs did not evolve by point mutations of a narrow-spectrum b-lactamase, the most impor- tant group being the CTX-M enzymes, which comprise at least 50 variants distributed in five subgroups represented by CTX-M-1, CTX-M-3, CTX-M-8, CTX-M-9, and CTX-M-25. The otherESBLs identified so far in Gram-negative bacteria are the VEB, PER and GES b-lactamases and, in addition, a series of rarely reported enzymes, e.g., BES-1, BEL-1, TLA-1 and TLA-2, and SFO-1.Several GES variants have weak but significant carbapenemase activity. This review considers the genetic bases of ESBL gene acquisition.
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