These techniques are not always available or affordable in resource-poor settings. Therefore, the prevalence of β-lactamases in developing countries is largely undetermined and the use of β-lactam antibiotics CAL-101 solubility dmso in such countries remains largely empiric. Based on resistance to β-lactam/β-lactamase inhibitor antibiotics, bacteria strains may be conveniently categorized into various resistant

phenotypes [5]. Strains exhibiting Narrow Spectrum β-lactamase Phenotypes (NSBLs) normally produce TEM-1 and/or SHV-1 enzymes that effectively degrade penicillins but are susceptible to other classes of β-lactams [6]. However, mutations on the promoter region of the gene encoding TEM-1 may result to over-production of these otherwise narrow-spectrum enzymes. This overproduction may in turn confer resistance to other classes of β-lactams besides penicillins [7–10]. Point mutations on these enzymes may also generate inhibitor resistant Crenigacestat manufacturer enzymes such as the Inhibitor Resistant TEMs (IRTs) that degrade penicillins but are not impeded by β-lactamase inhibitors such clavulanic acid or sulbactam [4, 11]. Extended Spectrum β-Lactamases (ESBLs) may also be derived from TEM- and SHV-type enzymes. ESBLs

exhibit a wide hydrolytic ability to different generations of cephalosporins but remain susceptible to β-lactamase inhibitors [12]. Complex Mutant TEMs (CMTs) are also derived from TEM-1 or TEM-2 and degrade most β-lactams but are susceptible to β-lactamase inhibitors including tazobactam. The CMTs are

also susceptible to cephamycins and carbapenems [13]. Plasmid–encoded AmpC (pAmpC) such as CMYs mediate resistance to most classes of β-lactams selleck screening library except to fourth generation cephalosporins and carbapenems Etomidate [14]. The β-lactamases with the worst clinical implications are those that degrade carbapenems, the most potent class of β-lactam antibiotics available today. Some carbapenemases such as the Klebsiella pneumoniae carbapenemases (KPC) degrade virtually all classes of β-lactams [15–17]. Some carbapenemases such as metallo-β-lactamases (MBLs) are however susceptible to aztreonam, a monobactam [18]. It is therefore clear that determination of β-lactamase phenotypes may not only aid the choice of agents to treat patients but may also guide the screening of bla genes and therefore save costs in surveillance studies. Understanding molecular epidemiology of bla gene is also important because majority of broad-spectrum resistant enzymes, especially the ESBLs and CMYs are encoded in conjugative plasmids that may be acquired across species barrier. Therefore, such genes have a high potential for spread via horizontal gene transfer mechanisms [19–22]. The phenotypic diversity of β-lactamase-producers in Kenya is poorly described and the diversity of bla genes has not been properly investigated [23–28].