AI Article Synopsis
- Atypical enteropathogenic Escherichia coli (aEPEC) show diversity in serotypes, adherence patterns, and virulence factors, which are essential for understanding their characteristics.
- The study analyzed the low-molecular mass proteomes of four aEPEC isolates with different adhesion phenotypes using 2D gel electrophoresis and LC-MS/MS techniques.
- A total of 59 proteins were identified, primarily linked to metabolism, protection, and transport, with many proteins being hypothetical or associated with enterohemorrhagic E. coli, emphasizing their role in key metabolic pathways.
Article Abstract
Atypical enteropathogenic Escherichia coli (aEPEC) are heterogeneous in terms of serotypes, adherence patterns and the presence of non-locus of enterocyte effacement virulence factors. In this study, the low-molecular mass proteomes of four representative aEPEC, comprising three different adhesion phenotypes (localized-like, aggregative and diffuse) and one non-adherent isolate, were analyzed and compared by 2D gel electrophoresis and LC-MS/MS. By mass spectrometry, a total of 59 proteins were identified according to their annotated function, with most of them being involved in metabolism, protection, and transport; some of them still classified as hypothetical proteins. Thus, in this comparative proteomic analysis of low-molecular mass extracted proteins from different aEPEC isolates, the proteins identified are mainly involved in key metabolic pathways. Also, the majority of the hypothetical and filamentous proteins identified in the isolates studied are products of genes originally identified in the genome of enterohemorrhagic E. coli.
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| http://dx.doi.org/10.1016/j.cimid.2012.06.001 | DOI Listing |
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