Amino-terminally Truncated forms of IpgC Retain Chaperone Activity for IpaB. Full-length and various truncated forms of IpgC were coexpressed with IpaB58-357 in recombinant strains of E. coli. Following induction of protein expression, cells were harvested, lysed, and the soluble extracts thereof were subjected to a copurification protocol to assess the ability of IpgC to bind IpaB. SDS-PAGE was used to analyze various protein samples following each step of copurification: M, protein molecular weight standards; E, clarified cellular extract following microfluidization and centrifugation; N, pooled elute following Ni2+-Sepharose chromatography; G, pooled fractions of the complex following gel-filtration chromatography. Since IpaB accumulates in inclusion bodies in the absence of IpgC activity, and since the untagged IpaB lacks the ability to bind Ni2+-NTA Sepharose on its own, all four IpgC proteins used in this study maintain chaperone activity.