Helicobacter pylori and Campylobacter rectus share a common antigen.

AIM

The aim of this study was to investigate the presence of antigens with immunological cross-reactivity in periodontopathogenic bacteria and Helicobacter pylori, the pathogen associated with gastritis and peptic ulcers in human.

MATERIALS AND METHODS/RESULTS: Among the putative periodontopathogens tested (Actinobacillus actinomycetemcomitans, Campylobacter rectus, Fusobacterium nucleatum, Porphyromonas gingivalis, Prevotella intermedia and Treponema denticola), cross-reactive bands were only detected in C. rectus by SDS-PAGE/Western immunoblotting analysis using a polyclonal antibody directed to H. pylori cells. One of these cross-reactive antigens, a 64-kDa band antigen, also reacted with a monoclonal antibody directed to the human heat shock protein (HSP) 60. The N-terminal amino acid sequence of this C. rectus protein revealed a high degree of homology with corresponding regions of other HSPs belonging to the HSP60 family, indicating that the 64-kDa antigen was a GroEL protein. The nucleotide sequence of the C. rectus GroEL protein coded for a 547 amino acid protein with a predicted size of 57.8 kDa. Comparison of the alignment of the deduced amino acid sequence of the GroEL protein of C. rectus with that of H. pylori showed a high degree of similarity throughout its length (76.8%). GroEL protein from C. rectus possessed the ability to stimulate production of IL-6 by a confluent monolayer of human gingival epithelial cells and was cytotoxic when used at a high concentration.

CONCLUSIONS

This study reveals an immunological relationship between H. pylori and C. rectus, and clearly indicates that one of the shared antigens is a GroEL protein possessing a biological activity that might play a role in the initiation and progression of periodontal disease.