J Periodontal Implant Sci.
2011 Apr;41(2):54-59.
Identification of mono- or poly-specific monoclonal antibody to Porphyromonas gingivalis heat-shock protein 60
- Affiliations
-
- 1Department of Periodontology, Pusan National University School of Dentistry, Yangsan, Korea. jrapa@pusan.ac.kr
- 2Department of Biochemistry, Pusan National University School of Medicine, Yangsan, Korea.
- 3Department of Pharmacology, Pusan National University School of Medicine, Yangsan, Korea.
- 4Department of Microbiology and Immunology, Seoul National University School of Dentistry, Seoul, Korea.
Abstract
- PURPOSE
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.
METHODS
In 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.
RESULTS
Five 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).
CONCLUSIONS
Peptide #19 and #29 of P. gingivalis HSP 60 might be important immunoreactive epitopes in the immunopathogenic mechanism of bacterial antigen-triggered autoimmune diseases.