Comparison of the proteome of uropathogenic E. coli 132

Objective To study proteome variation between uropathogenic E. coil (UPEC)132, UPEC J96 and non-uropathogenic E. coli K-12 MG1655. Methods Two-dimensional gel electrophoresis(2-DE) was applied to compare the differential expression proteins between UPEC 132, UPEC J96 and non-uro-pathogenic E.coli K-12 MG1655. The differential expression proteins were digested in gel by enzyme. The mass of generated peptides were measured by matrix assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS). The data obtained from peptide mass fingerprinting (PMF) were re-searched using the internet available database. Results The number of protein spots recognized from UPEC 132 was 466±11, significantly more than that of E. coli K-12 MG1655 (338±15) and UPEC J96 (382±12); there were 298 protein spots shared by the three E.coli strains, 56 protein spots shared by two UPEC strains, and 89 protein spots characterized by UPEC 132. Twenty-two differential expression or significantly increased expression protein spots, involved in virulence factors, metabolism and transportation, regulation of protein synthesis, biological oxidation and unknown functions, were successfully identified by MALDI-TOF-MS. Condusion The proteome from UPEC 132 and non-uropathogenic E. coli K-12 MG1655, or UPEC 132 and UPEC J96 was differentially expressed. It will provide important information on the pathogen-esis of UPEC 132. Key words: Uropathogenic E. coli;  Comparative proteomics