Purification of truncated and mutated Chemotaxis Inhibitory Protein of Staphylococcus aureus-an anti-inflammatory protein

The folding and biological activity of the purified proteins were analyzed by circular dichroism (CD) spectroscopy and flow cytometry, respectively, and compared to solubly produced CHIPS31-113 and wild-type CHIPS1-121. We show that the CHIPS variants produced in inclusion bodies can be refolded and purified to achieve equal biological activity as solubly produced CHIPS31-113 and wild-type CHIPS1-121. The truncation causes minor structural changes while purification from inclusion bodies or the soluble fraction does not further affect the structure.