The Escherichia coli ferric hydroxamate uptake receptor FhuA serves as the receptor for ferrichrome-Fe(III) complexes, with TonB protein energizing the active transport of the complex. The FhuA receptor is exploited by a variety of bacteriophages as a conduit into the cell. Interestingly, certain of these phages carry a gene called “Cor”, the product of which, when cloned and expressed from a plasmid, blocks transport by FhuA. In the present study, components of the cor gene from the bacteriophage ϕ80 were used to construct an IPTG-inducible MalE-Cor-His6 fusion protein, which allowed for affinity purification of the Cor protein. At 61 residues in length, purified Cor protein was not readily demonstrable by standard SDS polyacrylamide gel electrophoresis. The purification of Cor protein via maltose-binding and nickel exchange chromatography as well as visualization of Cor protein by silver staining of samples resolved on Tricine-SDS polyacrylamide gels is described.
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Brown, Alec, "Purification of a Bacteriophage Protein Involved in Host Range Specificity" (2016). Honors Projects. 724.