Hydrolytic activity of OXA and CTX-M beta-Lactamases against beta-Lactamic antibiotics

Abstract

Beta-Lactamases OXA and CTX-M are highly disseminated and confer resistance to antibiotics. This project gathers, classifies and analyzes information from indexed articles and databases as UNIPROT, EMBL and PDB, in order to correlate molecular data with activity profile of beta-lactamases against beta-Lactamic antibiotics. Sequences of CTX-M and OXA enzymes are analyzed by ClustalW multiple alignment and distance trees are built by Neighbor - joining with default parameters and a Bootstrap of 1000, through MEGA 5.0. Results from analysis were systematized with BLA.id system which documented 125 CTX-M, organized into four groups. Results show that CTX-M have punctual variations which change their hydrolytic activity profile. 310 OXAS grouped in 11 sets were analyzed and they show a high degree of conservation. Punctual changes in amino acids are correlated to changes in hydrolytic activity. BLA.id system fills a void in information about beta-Lactamases activity, which is disperse. © Springer International Publishing Switzerland 2014.