Identification of mono- or poly-specific monoclonal antibody to Porphyromonas gingivalis heat-shock protein 60.
10.5051/jpis.2011.41.2.54
- Author:
Jeomil CHOI
1
;
Sang Yull LEE
;
Koanhoi KIM
;
Bong Kyu CHOI
;
Myung Jin KIM
Author Information
1. Department of Periodontology, Pusan National University School of Dentistry, Yangsan, Korea. jrapa@pusan.ac.kr
- Publication Type:Original Article
- Keywords:
Antibodies;
Periodontitis;
Porphyromonas gingivalis
- MeSH:
Amino Acids;
Antibodies;
Antibodies, Monoclonal;
Autoimmune Diseases;
Chaperonin 60;
Clone Cells;
Cloning, Organism;
Epitopes;
Heat-Shock Proteins;
Humans;
Hybridomas;
Peptides;
Periodontitis;
Porphyromonas;
Porphyromonas gingivalis;
Sensitivity and Specificity
- From:Journal of Periodontal & Implant Science
2011;41(2):54-59
- CountryRepublic of Korea
- Language:English
-
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.
