The aim of this study was to define the immunoreactive specificity of Porphyromonas gingivalis ( P. gingivalis ) heat shock protein (HSP) 60 in periodontitis and atherosclerosis.
MethodsIn an attempt to define the cross-reactive bacterial heat-shock protein with human self-antigen at molecular level, we have introduced a novel strategy for cloning hybridoma producing anti- P. gingivalis HSP 60 which is polyreactive to bacterial HSPs or to the human homolog.
ResultsFive cross-reactive clones were obtained which recognized the #19 peptide (TLVVNRLRGSLKICAVKAPG) among 37 synthetic peptides (20-mer, 5 amino acids overlapping) spanning the whole molecule of P. gingivalis HSP 60. We have also established three anti- P. gingivalis HSP 60 monoclonal antibodies demonstrating mono-specificity. These clones recognized the #29 peptide (TVPGGGTTYIRAIAALEGLK).
ConclusionsPeptide #19 and #29 of P. gingivalis HSP 60 might be important immunoreactive epitopes in the immunopathogenic mechanism of bacterial antigen-triggered autoimmune diseases.