Hinode D, Yoshioka M, Tanabe S, Miki O, Masuda K, Nakamura R
Department of Preventive Dentistry, School of Dentistry, University of Tokushima, Japan.
FEMS Microbiol Lett. 1998 Oct 1;167(1):1-6. doi: 10.1111/j.1574-6968.1998.tb13199.x.
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.