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CTX-M-140 contained an alanine-to-threonine substitution at position 109 compared to its putative progenitor, CTX-M-14. When it was expressed in an\n Escherichia coli<\/jats:named-content>\n isogenic background, CTX-M-140 conferred 4- to 32-fold lower MICs of cephalosporins than those with CTX-M-14, indicating that the phenotype was attributable to this single substitution. For four mutants of CTX-M-14 that were constructed by site-directed mutagenesis (A109E, A109D, A109K, and A109R mutants), MICs of cephalosporins were similar to those for the\n E. coli<\/jats:named-content>\n host strain, which suggested that the alanine at position 109 was essential for cephalosporin hydrolysis. The kinetic properties of native CTX-M-14 and CTX-M-140 were consistent with the MICs for the\n E. coli<\/jats:named-content>\n clones. Compared with that of CTX-M-14, a lower hydrolytic activity against cephalosporins was observed for CTX-M-140.\n bla<\/jats:italic>\n CTX-M-140<\/jats:sub>\n is located on the chromosome as determined by I-CeuI pulsed-field gel electrophoresis (I-CeuI-PFGE) and Southern hybridization. The genetic environment surrounding\n bla<\/jats:italic>\n CTX-M-140<\/jats:sub>\n is identical to the sequence found in different plasmids with\n bla<\/jats:italic>\n CTX-M-9-group<\/jats:sub>\n genes among the\n Enterobacteriaceae<\/jats:named-content>\n . Genome sequencing and analysis showed that\n P. mirabilis<\/jats:named-content>\n strains with\n bla<\/jats:italic>\n CTX-M-140<\/jats:sub>\n have a genome size of \u223c4 Mbp, with a GC content of 38.7% and 23 putative antibiotic resistance genes. Our results indicate that alanine at position 109 is critical for the hydrolytic activity of CTX-M-14 against oxyimino-cephalosporins.\n <\/jats:p>","DOI":"10.1128\/aac.00822-16","type":"journal-article","created":{"date-parts":[[2016,8,2]],"date-time":"2016-08-02T03:04:34Z","timestamp":1470107074000},"page":"6121-6126","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":8,"title":["Characterization of CTX-M-140, a Variant of CTX-M-14 Extended-Spectrum \u03b2-Lactamase with Decreased Cephalosporin Hydrolytic Activity, from Cephalosporin-Resistant Proteus mirabilis"],"prefix":"10.1128","volume":"60","author":[{"given":"Guo-Bao","family":"Tian","sequence":"first","affiliation":[{"name":"Program of Immunology, Affiliated Guangzhou Women and Children's Medical Center, Zhongshan School of Medicine, Sun Yat-sen University, Guangzhou, China"},{"name":"Department of Immunology, Institute of Human Virology, Zhongshan School of 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