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Identification of mono- or poly-specific monoclonal antibody to Porphyromonas gingivalis heat-shock protein 60

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 molecu...

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Detalles Bibliográficos
Autores principales: Choi, Jeomil, Lee, Sang-Yull, Kim, Koanhoi, Choi, Bong-Kyu, Kim, Myung-Jin
Formato: Texto
Lenguaje:English
Publicado: Korean Academy of Periodontology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3087075/
https://www.ncbi.nlm.nih.gov/pubmed/21556254
http://dx.doi.org/10.5051/jpis.2011.41.2.54
Descripción
Sumario: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.