Journal of Periodontal and Implant Science

Korean Academy of Periodontology (대한치주과학회)
권호 표지

Development of monoclonal antibody against Porphyromonas gingivalis heat shock protein

Porphyromonas gingivali의 열충격단백-특이성 단클론항체의 개발

  • Yi, Ni-Na (Department of Periodontology, College of Dentistry, Pusan National University) ;
  • Lee, Ju-Youn (Department of Periodontology, College of Dentistry, Pusan National University) ;
  • Kim, Sung-Jo (Department of Periodontology, College of Dentistry, Pusan National University) ;
  • Choi, Jeom-II (Department of Periodontology, College of Dentistry, Pusan National University)
  • 이니나 (부산대학교 치과대학 치주과학교실) ;
  • 이주연 (부산대학교 치과대학 치주과학교실) ;
  • 김성조 (부산대학교 치과대학 치주과학교실) ;
  • 최점일 (부산대학교 치과대학 치주과학교실)
  • Published : 2007.03.30
Download PDF
⟨ Previous Next ⟩

Abstract

Heat shock protein (HSP) is one of cellular protein commonly present in major periodontopathogenic bacteria as well as mammalian cells. The protein may play a role in the immunopathogenesis by modulating autoimmune reaction due to its high level of sequence homology between bacteria and human counterpart. Hence, identifying immunodomiant epitope of bacteria HSP that is cross-reactive to periodontopathogenic bacteria with a specificity to human HSP may comprise a critical strategy for development of a periodontal vaccine. The present study was performed to establish clones producing monoclonal antibody reactive to Porphyromonas gingivalis (p. gingivalis) HSP with a specificity to human HSP. 4 different hybridomas were cloned producing monoclonal IgG antibodies to P, gingivalis HSP and evaluated for their reactivity and specificity to other periodontopathogenic bacteria as well as to human HSP. These four monoclonal antibodies reacted with p. gingivalis HSP only with specificities to other bacteria tested and human HSP as well. The antigenic epitopes producing the 4 monoclonal antibody may be potentially developed as vaccine candidates. Further investigations are under way to identify more clones producing monoclonal antibodies reactive to P, gingivalis HSP and to other periodontopathogenic bacteria as well, while maintaining specificities to human counterpart.

Keywords

References

  1. Taubman MA, Yoshie H, Wetherell JR, Ebersole JL, Smith DJ. Immune response and periodontal bone loss in germfree rats immunized with and infected with Actinobacillus actinomycetemcomitans. J Periodont Res 1983;18:393-401 https://doi.org/10.1111/j.1600-0765.1983.tb00375.x
  2. Klausen B. Microbiological and immunological aspects of experimental periodontal disease in rats: A review article. J Periodontol 1991:62:59-73 https://doi.org/10.1902/jop.1991.62.1.59
  3. Klausen B, Evans RT, Ramamurthy NS et al, Periodontal bone level and gingival proteinase activity in gnotobiotic rats immunized with Bacteroides gingivalis, Oral Microbial Immunol 1991:6:193-201 https://doi.org/10.1111/j.1399-302X.1991.tb00477.x
  4. Genco CA, Kapczynski DR, Cutler CW, Arko RJ, Arnold RR. Influence of immunization on Porphyromonas gingivahs colonization and invasion in the mouse chamber model. Infect Immun 1992:60:1447-1454
  5. Choi JI, Schifferle RE, Yoshimura F, Kim BW. Capsular polysaccharide-fimbrial protein conjugate vaccine protects against Porphyromonss gingivalis infection in SCID mice reconstituted with human peripheral blood lymphocytes. Infect Immun 1998:66: 391-393
  6. Katz J, Black KP, Michalek SM. Host responses to recombinant hemagglutinin B of Porphyromonas gingivalis in an experimental rat model. Infect Immun 1999:62:4352-4359
  7. Rajapakse PS. OBrien-Simpson NM, Slakeski N, Hoffman B, Reynolds EC. Immunization with the RgpA-Kgp proteinase-adhesin complexes of Porphyromonas gingivalis protects against bone loss in the rat periodontitis model. Infect Immun 2002: 70: 2480-2486 https://doi.org/10.1128/IAI.70.5.2480-2486.2002
  8. DeCarlo AA, Huang Y, Collyer CA, Langley DB, Katz J. Feasibility of an HA2 domain-based periodontitis vaccine. Infect Immun 2003:71:562-566 https://doi.org/10.1128/IAI.71.1.562-566.2003
  9. Page RC. The humoral response in patients with periodontitis: Effects of treatment and prospects for a vaccine. Compend Conti Educ Dent Suppl, 1994: No.18: S666-S671
  10. Dzink JL, Socransky SS, Haffajee AD. The predominant cultivable microbiota of active and inactive lesions of destructive periodontal disease. J Clin Periodontol 1998:15: 316-323
  11. Podmore M, Ebersole JL, Kinane DF. Immunodominant antigens in periodontal disease: a real or illusive concept? Crit Rev Oral Biol Med 2001:12:179-185 https://doi.org/10.1177/10454411010120020701
  12. Choi JI, Choi KS, Yi NN et al, Recognition and phagocytosis of multiple periodontopathogenic bacteria by anti -Porphromonas gingivalis heat-shock protein 60 antisera. Oral Microbiol Immunol 2005;20:51-55 https://doi.org/10.1111/j.1399-302X.2005.00182.x
  13. Shinnick TM. Heat shock proteins as antigens of bacterial and parasitic pathogens. Curr Top Microbiol Immunol 1991:167: 145-160
  14. Hinode D, Nakamura R, Grenier D, Mayrand D. Cross-reactivity of specific antibodies directed to heat shock proteins from periodontopathogenic bacteria and of human origin. Oral Microbiol Immunol 1998:13:55-58 https://doi.org/10.1111/j.1399-302X.1998.tb00752.x
  15. Gmur R, Thurnheer T, Guggenheim B. Dominant cross-reactive antibodies generated during the response to a variety of oral bacterial species detect phosphorylcholine. J Dent Res 1999:78:77-85 https://doi.org/10.1177/00220345990780011201
  16. Schenkein HA, Gunsolley JC, Best AM et al, Antiphosphorylcholine antibody levels are elevated in humans with periodontal diseases. Infect Immun 1999 67 4814-4818
  17. Maeda H, Miyamoto M, Hongyo H et al, Heat shock protein 60(GroEL) from Porphyromonas gingivalis:molecular cloning and sequence analysis of its gene and purification of recombinant protein. FEMS Microbiol Lett 1994:119:129-135 https://doi.org/10.1111/j.1574-6968.1994.tb06879.x
  18. Minami J, Matsumoto S, Yamada T. Putative heat shock protein 70 gene from Actinobacillus actinomycetemcomitans: molecular cloning and sequence analysis of its gene. Oral Microbiol Immunol 1998:13:113-119 https://doi.org/10.1111/j.1399-302X.1998.tb00721.x
  19. Reid HI, Riggio MP. Identification and nucleotide sequence of heat shock protein 60(GroEL) gene of Bacteroides forsythus. DNA Seq 1998:9:359-364 https://doi.org/10.3109/10425179809008477
  20. Tsai JP, Shi W. Analysis of gene expression in Treponema denticola with differential display polymerase chain reaction. Oral Microbiol Immunol 2000:15:305-308 https://doi.org/10.1034/j.1399-302x.2000.150506.x
  21. Skar CK, Bakken V. The heat shock response of Fusobacterium nucleatum. Eur J Oral Sci 2001:109:402-408 https://doi.org/10.1034/j.1600-0722.2001.00107.x
  22. Hinode D, Yoshioka M, Tanabe S et al. The GroEL-like protein from Campylobacter rectus: immunological characterization and interleukin-6 and -8 induction in human gingival fibroblast, FEMS Microbiol Lett 1998:167:1-6 https://doi.org/10.1111/j.1574-6968.1998.tb13199.x
  23. Kadri R, Devine D, Ashraf W, Purification and functional analysis of the DnaK homologue from Prevotella intermedia OMZ 326. FEMS Microbiol Lett 1998 : 167 : 63-68 https://doi.org/10.1111/j.1574-6968.1998.tb13208.x
  24. Holt SC, Kesavalu L, Walker S, Genco CA Virulence factors of Porphyromonas gingivalis. Periodontol 2000 1999:20:168-238
  25. Choi JI, Kang HS, Park YM, Kim SJ, Kim US. Identification of T-cell epitopes of Porphyromonas gingivalis heat-shock-protein 60 in periodontitis. Oral Microbiol Immunol 2004:19:1-5 https://doi.org/10.1046/j.0902-0055.2002.00087.x
  26. Choi JI, Chung SW, Kang HS et al, Establishment of Porphyromonas gingivalis heat shock protein-specific T-cell lines from atherosclerosis patients. J Dent Res 2002:81(5) :344-348 https://doi.org/10.1177/154405910208100511
  27. Saito K, Katsuragi H, Mikami M et al, Increase of heat-shock protein and induction of gamma/delta T cells in peritoneal exudate of mice after injection of live Fusobacterium nucleatum, Immunology 1997: 90: 229-235 https://doi.org/10.1046/j.1365-2567.1997.00143.x
  28. Ando T, Kato T, Ishihara K, Ogiuchi H, Okuda K. Heat shock proteins in the human periodontal disease process, Microbiol Immunol 1995:39:321-327 https://doi.org/10.1111/j.1348-0421.1995.tb02208.x
  29. Lopartin DE, Shelburne CE, Van Poperin N, Kowalski CJ, Bagramian RA. Humoral immunity to stress proteins and periodontal disease, J Periodontol 1999:70:1185-1193 https://doi.org/10.1902/jop.1999.70.10.1185
  30. Ishihara K, Ando T, Kosugi M et al. Relationships between the onset of pustulosis palmaris et plantaris, periodontitis and bacterial heat shock proteins. Oral Microbiol Immunol 2000:15:232-237 https://doi.org/10.1034/j.1399-302x.2000.150404.x
  31. Choi JI, Chung SW, Kang HS et al Epitope mapping of Porphyromonas gingivalis heat-shock protein and human heat-shock protein in human atherosclerosis, J Dent Res 2004:83(12) :936-940 https://doi.org/10.1177/154405910408301209
  32. Hansson GK. Immune mechanism in atherosclerosis. Arterioscler Thromb Vasc Biol 2001:21:1876-1890 https://doi.org/10.1161/hq1201.100220
  33. Wick G, Perschinka H, Millonig G. Atherosclerosis as an autoimmune disease: an update. Trends Immunol 2001:22:665-669 https://doi.org/10.1016/S1471-4906(01)02089-0
  34. Ueki K, Tabeta K, Yoshie H, Yamazaki K. Self-heat shock protein 60 induces tumour necrosis factor-alpha in monocyte-derived macrophage : possible role in chronic inflammatory periodontal disease. Clin Exp Immunol 2002:127:72-77 https://doi.org/10.1046/j.1365-2249.2002.01723.x
  35. Yamazaki K, Ohsawa Y, Tabeta K et al, Accumulation of human heat shock protein 60-reactive T cell in the gingival tissues of periodontitis patients. Infect Immun 2002:70:2492-2501 https://doi.org/10.1128/IAI.70.5.2492-2501.2002