Expression and Purification of the Periplasmic Chaperone SurA

Science Center, Bent Corridor

SurA is a chaperone protein found in the periplasmic space of E. coli and other gram-negative bacteria. It has been shown to aid in the assembly and proper folding of outer-membrane proteins (OMPs) necessary for the proper function and, in some cases, increased pathogenicity of the bacteria. Inhibition of SurA using small molecules that bind to the active site of the protein could have downstream effects on the virulence of the bacteria. In order to study the inhibition of SurA, it is necessary to optimize an efficient and reliable process of overexpressing and purifying the protein itself. Using a five-step process of induction, lysis, affinity chromatography, distillation, and concentration, we have increased the amount of viable SurA that can be used for these experiments.