The native GroEL-like protein was purified from Campylobacter rectus, a putative periodontal pathogen, by affinity chromatography on ATP-agarose followed by high performance liquid chromatography on Superose 6. The purified 64-kDa protein (denatured form of GroEL-like protein) was immunoreactive by SDS-PAGE and Western immunoblotting with the monoclonal antibody directed against heat shock protein 60 of human origin. The native GroEL-like protein stimulated both interleukin-6 (IL-6) and IL-8 secretion by a confluent monolayer of human gingival fibroblast in their culture supernatant. During the 22-h incubation, the amounts of IL-6 and IL-8 were increased by 5.4- and 3.5-fold, respectively. These data suggested that the GroEL-like protein might be considered to be a virulence factor of C. rectus in periodontal disease. Copyright (C) 1998 Federation of European Microbiological Societies.
Hinode, D., Yoshioka, M., Tanabe, S. I., Miki, O., Masuda, K., & Nakamura, R. (1998). The GroEL-like protein from Campylobacter rectus: Immunological characterization and interleukin-6 and -8 induction in human gingival fibroblast. FEMS Microbiology Letters, 167(1), 1–6. https://doi.org/10.1016/S0378-1097(98)00359-0