Proteomic evaluation of Escherichia coli isolates from human clinical strains

DOI: 10.5584/jiomics.v1i1.20

Authors

  • Luís Pinto Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal; 2Institute for Biotechnology and Bioengineering, Centre of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal
  • Patrícia Poeta Veterinary Science Department, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal
  • Hajer Radhouani Veterinary Science Department, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal
  • Céline Coelho Veterinary Science Department, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal
  • Carlos Carvalho Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal
  • Jorge Rodrigues Centre of Studies of Animal and Veterinary Sciences, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal
  • Carmen Torres Biochemistry and Molecular Biology Area, University of Rioja, Logroño, Spain
  • Rui Vitorino Chemistry Department, University of Aveiro, Aveiro, Portugal
  • Pedro Domingues Chemistry Department, University of Aveiro, Aveiro, Portugal
  • Gilberto Igrejas Department of Genetics and Biotechnology, University of Trás-os-Montes and Alto Douro, Vila Real, Portugal

Abstract

Acquired resistance to beta-lactams is mainly mediated by extended-spectrum beta-lactamases (ESBLs) that confer bacterial resistance to all beta-lactams except carbapenems and cephamycins, which are inhibited by other beta-lactamase inhibitors such as clavulanic acid. Although ESBLs still constitute the first cause of resistance to beta-lactams among Escherichia coli, other “new beta-lactamases” conferring resistance to carbapenems, such as metallo-beta-lactamases (MBL) and KPC carbapenemases, or to cephamycins, such as CMY enzymes, have more recently emerged and are often associated with ESBLs. In order to identify and characterize the proteome of extended-spectrum β-lactamase (ESBL) type TEM-52 and CMY-2 producing-Escherichia coli strains of human clinical origin a bidimensional electrophoresis (2-DE) technique with an isoelectric focusing followed by a SDS-PAGE, were used.  Full proteomic studies were conducted in the same IEF and SDS-PAGE conditions, for two protein samples of E. colistrains with similar antibiotic-resistance profiles recovered from human clinical sources. A total of 64 and 91 spots were recovered and identified in C583 and C580 strains, respectively. Our results will be helpful for further understanding of antibiotic-resistant mechanism.

Published

2011-09-29