Abstract
Protein-protein interactions (PPIs) regulate most of the biological activities within a cell. A set of pairwise PPIs in seven genera of bacterial pathogens (Salmonella, Escherichia, Shigella, Yersinia, Klebsiella, Photorhabdus, and Pantoea) of Enterobacteriaceae family was analysed. At genotypic level, the correlation coefficient analysis of the mutation spectra of the ten sets of directly interacting protein partners in Escherichia coli recognised all the ‘interacting partners' in Escherichia coli. Extending the correlation analysis to include strains from the rest of the bacterial genera decreased the recognition efficiency providing quantitative evidence that binary interactome have incomplete superposition across species. At phenotype level, a reliable classification of bacterial pathogens was obtained by measuring PPI variations in terms of between phylogenetic distance correlation distances among ten sets of proteins partners. This forces us to rethink upon the possibility of PPI rewiring with a consequent change in physiological role of the same protein.
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