Polyclonal anti-idiotypic antibodies which mimic an epitope of the human prion protein

Molecular Immunology

Volumn 46, Issue 6, 2009, Pages 1076-1083

  Hanoux, Vincent ^a,b   Wijkhuisen, Anne ^a,b   Alexandrenne, Coralie ^a,b   Créminon, Christophe ^a   Boquet, Didier ^a   Couraud, Jean Yves ^a,b  

^a CEA SACLAY   (France)

^b UNIVERSITÉ PARIS DESCARTES   (France)

Author keywords

Anti idiotypic antibody; Antigen antibody interaction; Human prion protein; Immunotherapy; Molecular mimicry; Neurodegenerative disorders; Vaccination

Indexed keywords

CD3 ANTIGEN; EPITOPE; IDIOTYPIC ANTIBODY; LIGAND; MONOCLONAL ANTIBODY SAF61; POLYCLONAL ANTIBODY; PRION PROTEIN; PRION PROTEIN ANTIBODY; UNCLASSIFIED DRUG;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIGEN BINDING; ARTICLE; CONTROLLED STUDY; DRUG MECHANISM; EXPERIMENTAL RABBIT; FLOW CYTOMETRY; IMMUNOTHERAPY; MALE; MOUSE; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN PROTEIN INTERACTION; VACCINATION;

AMINO ACID SEQUENCE; ANIMALS; ANTIBODIES, ANTI-IDIOTYPIC; ANTIBODIES, MONOCLONAL; CELL LINE; EPITOPES; HUMANS; MICE; MOLECULAR MIMICRY; MOLECULAR SEQUENCE DATA; PEPTIDES; PRIONS; RABBITS;

ORYCTOLAGUS CUNICULUS;

EID: 60949088117     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.09.033     Document Type: Article

References (57)

1. Aguzzi A., and Sigurdson C.J. Antiprion immunotherapy: to suppress or to stimulate?. Nat. Rev. Immunol. 4 (2004) 725-736
2. Alfonso M., Diaz A., Hernandez A.M., Perez A., Rodriguez E., Bitton R., Perez R., and Vazquez A.M. An anti-idiotype vaccine elicits a specific response to N-glycolyl sialic acid residues of glycoconjugates in melanoma patients. J. Immunol. 168 (2002) 2523-2529
3. Attanasio R., Kennedy R.C., Allan J.S., Maino V.C., Buck D., and Kanda P. Anti-idiotypic antibodies of a predefined specificity generated against CDR3VH synthetic peptides define a private anti-CD4 idiotype. Mol. Immunol. 27 (1990) 513-522
4. Beninati C., Midiri A., Mancuso G., Biondo C., Arigo M., Gerace E., Papasergi S., Gambuzza M., Boretti M., Magliani W., Conti S., Polonelli L., and Teti G. Antiidiotypic DNA vaccination induces serum bactericidal activity and protection against group B meningococci. J. Exp. Med. 203 (2006) 111-118
5. Bhattacharya-Chatterjee M., and Kohler H. Anti-idiotype tumor vaccines. Adv. Exp. Med. Biol. 251 (1989) 113-127
6. Bhattacharya-Chatterjee M., Chatterjee S.K., and Foon K.A. Anti-idiotype vaccine against cancer. Immunol. Lett. 74 (2000) 51-58
7. Bhattacharya-Chatterjee M., Nath Baral R., Chatterjee S.K., Das R., Zeytin H., Chakraborty M., and Foon K.A. Counterpoint. Cancer vaccines: single-epitope anti-idiotype vaccine versus multiple-epitope antigen vaccine. Cancer Immunol. Immunother. 49 (2000) 133-141
8. Bhattacharya-Chatterjee M., Chatterjee S.K., and Foon K.A. The anti-idiotype vaccines for immunotherapy. Curr. Opin. Mol. Ther. 3 (2001) 63-69
9. Boquet D., Déry O., Frobert Y., Grassi J., and Couraud J.Y. Is hydropathic complementarity involved in antigen-antibody binding?. Mol. Immunol. 32 (1995) 303-308
10. Bret-Dibat J.L., Zouaoui D., Déry O., Zerari F., Grassi J., Maillet S., Conrath M., and Couraud J.Y. Antipeptide polyclonal antibodies that recognize a substance P-binding site in mammalian tissues: a biochemical and immunocytochemical study. J. Neurochem. 63 (1994) 333-343
11. Chatterjee S.K., Tripathi P.K., Chakraborty M., Yannelli J., Wang H., Foon K.A., Maier C.C., Blalock J.E., and Bhattacharya-Chatterjee M. Molecular mimicry of carcinoembryonic antigen by peptides derived from the structure of an anti-idiotype antibody. Cancer Res. 58 (1998) 1217-1224
12. Checler F., and Vincent B. Alzheimer's and prion diseases: distinct pathologies, common proteolytic denominators. Trends Neurosci. 25 (2002) 252-261
13. Diaz A., Alfonso M., Alonso R., Saurez G., Troche M., Catala M., Diaz R.M., Perez R., and Vazquez A.M. Immune responses in breast cancer patients immunized with an anti-idiotype antibody mimicking NeuGc-containing gangliosides. Clin. Immunol. 107 (2003) 80-89
14. De Cerio A.L., Zabalegui N., Rodriguez-Calvillo M., Inoges S., and Bendandi M. Anti-idiotype antibodies in cancer treatment. Oncogene 26 (2007) 3594-3602
15. Enari M., Flechsig E., and Weissman C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion antibody. Proc. Natl. Acad. Sci. U.S.A. 98 (2001) 9295-9299
16. Feng Z., Qiu Z., Li Y., Li Y., Zhu C., Xue W., and Guan X. Protective immunity induced by the anti-idiotypic monoclonal antibody NP30 of Schistosoma japonicum. Chin. Med. J. (Engl.) 115 (2002) 576-579
17. Féraudet C., Morel N., Simon S., Volland H., Frobert Y., Créminon C., Vilette D., Lehman S., and Grassi J. Screening of 145 anti-PrP monoclonal antibodies for their capacity to inhibit PrPSc replication in infected cells. J. Biol. Chem. 280 (2005) 11247-11258
18. Fernandez-Borges N., Brun A., Whitton J.L., Parra B., Diaz-San Segundo F., Salguero F.J., Torres J.M., and Rodriguez F. DNA vaccination can break immunological tolerance to PrP in wild-type mice and attenuates prion disease after intracerabral challenge. J. Virol. 80 (2006) 9970-9976
19. Foon K.A., John W.J., Chakraborty M., Das R., Teitelbaum A., Garrison J., Kashala O., Chatterjee S.K., and Bhattacharya-Chatterjee M. Clinical and immune responses in resected colon cancer patients treated with anti-idiotype monoclonal antibody vaccine that mimics the carcinoembryonic antigen. J. Clin. Oncol. 9 (1999) 2889-2895
20. Grassi J., Frobert Y., Pradelles P., Chercuitte F., Gruaz D., Dayer J.M., and Poubelle P.E. Production of monoclonal antibodies against interleukin-1 alpha and -1 beta. Development of two enzyme immunometric assays (EIA) using acetylcholinesterase and their application to biological media. J. Immunol. Methods 123 (1989) 193-210
21. Guthmann M.D., Castro M.A., Cinot G., Venier C., Kolisen L., Bitton R.J., Vazquez A.M., and Fainboim L. Cellular en humoral immune response to N-Glycolyl-GM3 elicited by prolonged immunotherapy with an anti-idiotypic vaccine in high-risk and metastatic breast cancer patients. J. Immunother. 29 (2006) 215-223
22. Hanin V., Déry O., Boquet D., Sagot M.A., Créminon C., Couraud J.Y., and Grassi J. Importance of hydropathic complementary for the binding of the neuropeptide substance P to a monoclonal antibody: equilibrium and kinetic studies. Mol. Immunol. 34 (1997) 829-838
23. Hantusch B., Knittelfelder R., Wallmann J., Krieger S., Szalai K., Unstermayr E., Vogel M., Stadler B.M., Scheiner O., Boltz-Nitulescu G., and Jensen-Jarolim E. Internal images: human anti-idiotypic Fab antibodies mimic the IgE epitopes of grass pollen allergen Phlp 5a. Mol. Immunol. 43 (2006) 2180-2187
24. Jerne N.K. Towards a network theory of the immune system. Ann. Immunol. Paris 125C (1974) 373-389
25. 0/0 mice. J. Immunol. Methods 199 (1996) 109-118
26. Kyte J., and Doolitlle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 (1982) 102-132
27. Lefranc M.P., Giudicelli V., Kaas Q., Duprat E., Jabado-Michaloud J., Scaviner D., Ginestoux C., Clément O., Chaume D., and Lefranc G. IMGT, the international ImMunoGeneTics information system(R). Nucl. Acids Res. 33 (2005) D593-D597
28. Lehmann S., and Harris D.A. A mutant prion protein displays an aberrant membrane association when expressed in cultured cells. J. Biol. Chem. 270 (1995) 24589-24597
29. Levi M., Sallberg M., Rudtn U., Herlynt D., Maruyamat H., Wigzell H., Marks J., and Wahren B. A complementary-determining region synthetic peptide acts as a miniantibody and neutralizes human immunodeficience virus type 1 in vitro. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 4374-4378
30. Ma J., Wollmann R., and Lindquist S. Neurotoxicity and neurodegeneration when PrP accumulates in the cytosol. Science 298 (2002) 1781-1785
31. Magliani W., Conti S., Frazzi R., Ravanetti L., Maffei D.L., and Polonelli L. Protective antifungal yeast killer toxin-like antibodies. Curr. Mol. Med. 5 (2005) 443-452
32. Maier C.C., Moseley H.N., Zhou S.R., Whitaker J.N., and Blalock J.E. Identification of interactive determinants on idiotypic-anti-idiotypic antibodies through comparison of their hydropathic profiles. Immunomethods 5 (1994) 107-113
33. Martins V.R., Graner E., Garcia-Abreu J., de Souza S.J., Mercadante A.F., Veiga S.S., Zanata S.M., Neto V.M., and Brentani R.R. Complementary hydropathy identifies a cellular prion protein receptor. Nat. Med. 3 (1997) 1376-1382
34. Morel N., Simon S., Frobert Y., Volland H., Mourton-Gilles C., Negro A., Sorgato M.C., Créminon C., and Grassi J. Selective and efficient immunoprecipitation of the disease-associated form of the prion protein can be mediated by nonspecific interactions between monoclonal antibodies and scrapies-associated fibrils. J. Biol. Chem. 279 (2004) 30143-30149
35. Murray J.L., Gillogly M., Kawano K., Efferson C.L., Lee J.E., Ross M., Wang W., Ferrones S., and Ioannides C.G. Fine specificity of high molecular weight-melanoma-associated antigen-specific cytotoxic T lymphocytes elicited by anti-idiotypic monoclonal antibodies in patients with melanoma. Cancer Res. 64 (2004) 5481-5488
36. Nikles D., Bach P., Boller K., Merten C.A., Montrasio F., Heppner F.L., Aguzzi A., Cichutek K., Kalinke U., and Buchholz C.J. Circumventing tolerance to the prion protein (PrP): vaccination with PrP-displaying retrovirus particles induces humoral immune responses against the native form of cellular PrP. J. Virol. 79 (2005) 4033-4042
37. Padiolleau-Lefevre S., Alexandrenne C., Dkhissi F., Clément G., Essono S., Blache C., Couraud J.Y., Wijkhuisen A., and Boquet D. Expression and detection strategies for an scFv fragment retaining the same high affinity than Fab and whole antibody: implications for therapeutic use in prion diseases. Mol. Immunol. 44 (2007) 1888-1896
38. Peretz D., Williamson R.A., Kaneko K., Vergara J., Leclerc E., Schmitt-Ulms G., Mehlhorn I.R., Legname G., Wormald M.R., Rudd P.M., Dwek R.A., Burton D.R., and Prusiner S.B. Antibodies inhibit prion propagation and clear cell cultures of prion infectivity. Nature 412 (2001) 739-743
39. Perrier V., Solassol J., Crozet C., Frobert Y., Mourton-Gilles C., Grassi J., and Lehmann S. Anti-PrP antibodies block PrPSc replication in prion-infected cell cultures by accelerating PrPC degradation. J. Neurochem. 89 (2004) 454-463
40. Pfisterer J., du Bois A., Sehouli J., Loibl S., Reinartz S., Reuss A., Canzler U., Belau A., Jackisch C., Kimmig R., Wollschlaeger K., Heilmann V., and Hilpert F. The anti-idiotypic antibody abagovomab in patients with recurrent ovarian cancer. A phase I trial of the AGO-OVAR. Ann. Oncol. 17 (2006) 1568-1577
41. Pride M.W., Shi H., Anchin J.M., Linthicum D.S., LoVerde P.T., Thakur A., and Thanavala Y. Molecular mimicry of hepatitis B surface antigen by an anti-idiotype-derived synthetic peptide. Proc. Natl. Acad. Sci. U.S.A. 89 (1992) 11900-11904
42. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science 216 (1982) 136-144
43. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 13363-13383
44. Rezaei H., Marc D., Choiset Y., Takahashi M., Hui Bon Hoa G., Haertlé T., Grosclaude J., and Debey P. High yield purification and physico-chemical properties of full-length recombinant allelic variants of sheep prion protein linked to scrapie susceptibility. Eur. J. Biochem. 267 (2000) 2833-2839
45. Sabbatini P., Dupont J., Aghanian C., Derosa F., Poynor E., Anderson S., Hensley M., Livingston P., Iasonos A., Spriggs D., McGuire W., Reinartz S., Schneider S., Grande C., Lele S., Rodabaugh K., Kepner J., Ferrone S., and Odunsi K. Phase I study of abagovomab in patients with epithelial ovarian, fallopian tube, or primary peritoneal cancer. Clin. Cancer Res. 12 (2006) 5503-5510
46. Sagot M.A., Wijkhuisen A., Créminon C., Tymciu S., Frobert Y., Turbica I., Grassi J., Couraud J.Y., and Boquet D. A monoclonal antibody directed against the neurokinin-1 receptor contains a peptide sequence with a similar hydropathy and functional properties to substance P, the natural ligand for the receptor. Mol. Immunol. 37 (2000) 423-433
47. Sakudo A., Onodera T., Suganuma Y., Kobayashi T., Saeki K., and Ikuba K. Recent advances in clarifying prion protein functions using knockout mice and derived cell lines. Mini. Rev. Med. Chem. 6 (2006) 589-601
48. Shearer M.H., Dalgleish A.G., Chanh T.C., and Kennedy R.C. Idiotype cascades associated with the CD4-HIV glycoprotein 120 interaction: immunization with anti-idiotypic antibodies induces anti-anti-idiotypic responses with anti-CD4 specificity and in vitro neutralizing activity. AIDS Res. Hum. Retroviruses 16 (2000) 77-86
49. Shyng S.L., Lehmann S., Moulder K.L., and Harris D.A. Sulfated glycans stimulate endocytosis of the cellular isoform of the prion protein, PrPC, in cultured cells. J. Biol. Chem. 270 (1995) 30221-30229
50. Van Regenmortel M.H., and Pellequer J.L. Predicting antigenic determinants in protein: looking for unidimensional solutions to a three-dimensional problem?. Pept. Res. 7 (1994) 224-228
51. Von Feldt J.M., Kieber-Emmons T., Weiner D.B., Ugen K.E., and Williams W.V. Molecular structure and granulocyte/macrophage colony-stimulating factor activity. DNA Cell Biol. 11 (1992) 183-191
52. Watzlawik J., Skora L., Frense D., Griesinger C., Zweckstetter M., Schulz-Schaeffer W.J., and Kramer M.L. Prion protein helix1 promotes aggregation but is not converted into β-sheet. J. Biol. Chem. 281 (2006) 30242-30250
53. White A.R., Enever P., Tayebi M., Mushens R., Linehan J., Brandner S., Anstee D., Collinge J., and Hawke S. Monoclonal antibodies inhibit prion replication and delay the development of prion disease. Nature 422 (2003) 80-83
54. Wijkhuisen A., Sagot M.A., Frobert Y., Créminon C., Grassi J., Boquet D., and Couraud J.Y. Identification in the NK1 tachykinin receptor of a domain involved in recognition of neurokinin A and septide but not of substance P. FEBS Lett. 447 (1999) 155-159
55. Wijkhuisen A., Tymciu S., Fischer J., Alexandrenne C., Créminon C., Frobert Y., Grassi J., Boquet D., Conrath M., and Couraud J.Y. Pharmacological properties of peptides derived from an antibody against the tachykinin NK1 receptor for the neuropeptide substance P. Eur. J. Pharmacol. 468 (2003) 175-182
56. Xu J.L., and Davis M.M. Diversity in the CDR3 region of VH is sufficient for most antibody specificities. Immunity 13 (2000) 37-45
57. Yildirim T., Basalp A., Yücel F., Manav A.I., and Sezen I.Y. Generation of anti-idiotypic antibodies that mimic HbsAg and vaccination against hepatitis B virus. Hybrid. Hybridomics 23 (2004) 192-197