Using a single-run protein-mapping technique, biologists have mapped a number of key proteins in a specific strain of Escherichia coli , various strains of which harmlessly thrive in the human gut1.
This knowledge will form a base for the identification of changes in proteins in harmful strains of this bacterium, providing leads for the development of antibacterial therapies.
The single-run protein-mapping technique has already been used to map proteins in yeast and different mammalian cells. To test its potential in mapping proteins in bacteria, scientists from the Centre for Cellular and Molecular Biology, and the National Institute of Pharmaceutical Education and Research in Hyderabad, India, worked with a few micrograms of bacterial proteins extracted from a specific strain of E. coli grown on a nutrient broth.
They identified 2068 proteins that drive important cellular and signalling pathways in the bacteria. The proteins include highly expressed proteins such as outer-membrane protein, DNA-binding protein, glyceraldehydes-3-phosphate dehydrogenase and low-abundant proteins such as ATP-binding protein, glycerate kinase and lipoproteins.
The quantified proteins are about 52% of the total proteins present in E. coli genome. Besides mapping proteins linked to different molecular pathways, this method identified protein-protein interactions, making it potentially useful for understanding the complex cellular system of E. coli .
The researchers say that this method could be applied to map proteins in pathogenic strains of E. coli that cause diarrhoea and diseases affecting the kidneys and the brain.