Conformation of PrPC on the cell surface as probed by antibodies

Journal of Molecular Biology

Volumn 326, Issue 2, 2003, Pages 475-483

  Leclerc, Estelle ^a   Peretz, David ^b,c   Ball, Haydn ^b   Solforosi, Laura ^a   Legname, Giuseppe ^b,c   Safar, Jiri ^b,c   Serban, Ana ^b   Prusiner, Stanley B ^b,c   Burton, Dennis R ^a   Williamson, R Anthony ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

Antibody; Cell surface; Conformational change; Flow cytometry; Prion protein (PrP)

Indexed keywords

EPITOPE; IMMUNOGLOBULIN F(AB) FRAGMENT; MONOCLONAL ANTIBODY; PRION PROTEIN;

ALPHA HELIX; AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANIMAL EXPERIMENT; ANTIBODY LABELING; ANTIGEN ANTIBODY REACTION; ANTIGEN RECOGNITION; ARTICLE; BINDING COMPETITION; CARBOXY TERMINAL SEQUENCE; CELL MEMBRANE; CELL SURFACE; CHO CELL; CONTROLLED STUDY; GENETIC TRANSFECTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN PROTEIN INTERACTION; SYRIAN HAMSTER; TITRIMETRY;

CRICETINAE; MESOCRICETUS AURATUS;

EID: 0037436344     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01365-7     Document Type: Article

References (54)

1. Bolton D.C., McKinley M.P., Prusiner S.B. Identification of a protein that purifies with the scrapie prion. Science. 218:1982;1309-1311.
2. Prusiner S.B. Molecular biology of prion diseases. Science. 252:1991;1515-1522.
3. Weissmann C., Fischer M., Raeber A., Bueler H., Sailer A., Shmerling D., et al. The role of PrP in pathogenesis of experimental scrapie. Cold Spring Harbor Symp. Quant. Biol. 61:1996;511-522.
4. Prusiner S.B., Scott M.R., DeArmond S.J., Cohen F.E. Prion protein biology. Cell. 93:1998;337-348.
5. Weissmann C. Molecular genetics of transmissible spongiform encephalopathies. J. Biol. Chem. 274:1999;3-6.
6. Bendheim P.E., Brown H.R., Rudelli R.D., Scala L.J., Goller N.L., Wen G.Y., et al. Nearly ubiquitous tissue distribution of the scrapie agent precursor protein. Neurology. 42:1992;149-156.
7. Stahl N., Borchelt D.R., Hsiao K., Prusiner S.B. Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell. 51:1987;229-240.
8. Stahl N., Borchelt D.R., Prusiner S.B. Differential release of cellular and scrapie prion proteins from cellular membranes by phosphatidylinositol-specific phospholipase C. Biochemistry. 29:1990;5405-5412.
9. Donne D.G., Viles J.H., Groth D., Mehlhorn I., James T.L., Cohen F.E., et al. Structure of the recombinant full-length hamster prion protein PrP(29-231): the N terminus is highly flexible. Proc. Natl Acad. Sci. USA. 94:1997;13452-13457.
10. Riek R., Hornemann S., Wider G., Glockshuber R., Wüthrich K. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Letters. 413:1997;282-288.
11. Lopez Garcia F., Zahn R., Riek R., Wüthrich K. NMR structure of the bovine prion protein. Proc. Natl Acad. Sci. USA. 97:2000;8334-8339.
12. Zahn R., Liu A., Luhrs T., Riek R., von Schroetter C., Lopez Garcia F., et al. NMR solution structure of the human prion protein. Proc. Natl Acad. Sci. USA. 94:2000;13452-13457.
13. Stockel J., Safar J., Wallace A.C., Cohen F.E., Prusiner S.B. Prion protein selectively binds copper (II) ions. Biochemistry. 37:1998;7185-7193.
14. Miura T., Hori-i A., Mototani H., Takeuchi H. Raman spectroscopic study on the copper(II) binding mode of prion octapeptide and its pH dependence. Biochemistry. 38:1999;11560-11569.
15. Viles J.H., Cohen E.F., Prusiner S.B., Goodin D.B., Wright P.E., Dyson H.J. Copper binding to the prion protein:structural implications of four identical cooperative binding sites. Proc. Natl Acad. Sci. USA. 96:1999;2042-2047.
16. Jackson G.S., Murray I., Hosszu L.L.P., Gibbs N., Waltho J.P., Clarke A.R., Collinge J. Location and properties of metal-binding sites on the human prion protein. Proc. Natl Acad. Sci. USA. 98:2001;8531-8535.
17. 91-231 and its low-resolution structure in solution. J. Mol. Biol. 311:2001;467-473.
18. Prusiner S.B., Groth D.F., Bolton D.C., Kent S.B., Hood L.E. Purification and structural studies of a major scrapie prion protein. Cell. 38:1984;127-134.
19. Rogers M., Yehiely F., Scott M., Prusiner S.B. Conversion of truncated and elongated prion proteins into the scrapie isoform in cultured cells. Proc. Natl Acad. Sci. USA. 90:1993;3182-3186.
20. Fischer M., Rulicke T., Raeber A., Sailer A., Moser M., Oesch B., et al. Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J. 15:1996;1255-1264.
21. Owen F., Poulter M., Lofthouse R., Collinge J., Crow T.J., Risby D., et al. Insertion in prion protein gene in familial Creutzfeldt-Jakob disease. Lancet. II:1989;51-52.
22. Goldfarb L.G., Brown P., McCombie W.R., Goldhaber D., Swergold G.D., Wills P.R., et al. Transmissible familial Creutzfeldt-Jakob disease associated with five, seven, and eight extra octapeptide coding repeats. Proc. Natl Acad. Sci. USA. 88:1991;10926-10930.
23. Poulter M., Baker H.F., Frith C.D., Leach M., Lofthouse R., Ridley R.M., et al. Inherited prion disease with 144 base pair gene insertion.1. Genealogical and molecular studies. Brain. 115:1992;675-685.
24. Beck J.A., Mead S., Campbell T.A., Dickinson A., Wientjens D.P.M.W., Croes M.D., et al. Two-octapeptide repeat deletion of prion protein associated with rapidly progressive dementia. Neurology. 57:2001;354-356.
25. Flechsig E., Shmerling D., Hegyi I., Raeber A.J., Fischer M., Cozzio A., et al. Prion devoid of the octapeptide repeat region restores susceptibility to scrapie in PrP knockout mice. Neuron. 27:2000;399-408.
26. Lawson V.A., Priola S.A., Wehrly K., Chesebro B. N-terminal truncation of prion protein affects both formation and conformation of abnormal protease-resistant prion protein generated in vitro. J. Biol. Chem. 276:2001;35265-35271.
27. Sc accumulation. J. Virol. 72:1998;1153-1159.
28. Chabry J., Caughey B., Chesebro B. Specific inhibition of in vitro formation of protease-resistant prion protein by synthetic peptides. J. Biol. Chem. 273:1998;13203-13207.
29. Chabry J., Priola S.A., Wehrly K., Nishio J., Hope J., Chesebro B. Species-independent inhibition of abnormal prion protein (PrP) formation by a peptide containing a conserved PrP sequence. J. Virol. 73:1999;6245-6250.
30. Peretz D., Williamson R.A., Matsunaga Y., Serban H., Pinilla C., Bastidas R.B., et al. A conformational transition at the N terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273:1997;614-622.
31. Williamson R.A., Peretz D., Pinilla C., Ball H., Bastidas R.B., Rozenshteyn R., et al. Mapping the prion protein using recombinant antibodies. J. Virol. 72:1998;9413-9418.
32. Leclerc E., Peretz D., Ball H., Sakurai H., Legname G., Serban A., et al. Immobilized prion protein undergoes spontaneous rearrangement to a conformation having features in common with the infectious form. EMBO J. 20:2001;1547-1554.
33. Telling G.C., Scott M., Mastrianni J., Gabizon R., Torchia M., Cohen F.E., et al. Prion propagation in mice expressing human and chimeric PrP transgenes implicates the interaction of cellular PrP with another protein. Cell. 83:1995;79-90.
34. Prusiner S.B. Current Topics in Microbiology and Immunology. Current Topics in Microbiology and Immunology. vol. 270:1996;Springer, Berlin.
35. Kaneko K., Zulianello L., Scott M., Cooper C.M., Wallace A.C., James T.L., et al. Evidence for protein X binding to a discontinuous epitope on the cellular prion protein during scrapie prion propagation. Proc. Natl Acad. Sci. USA. 94:1997;10069-10074.
36. Billeter M., Riek R., Wider G., Hornemann S., Glockshuber R., Wüthrich K. Prion protein NMR structure and species barrier for prion diseases. Proc. Natl Acad. Sci. USA. 94:1997;7281-7285.
37. Peretz D., Williamson R.A., Kaneko K., Vergara J., Leclerc E., Mehlhorn I.R., et al. Antibodies abolish prion propagation and promote clearance of infectivity from cell culture. Nature. 412:2001;739-743.
38. Enari M., Flechsig E., Weissmann C. Scrapie prion protein accumulation by scrapie-infected neuroblastoma cells abrogated by exposure to a prion protein antibody. Proc. Natl Acad. Sci. USA. 98:2001;9295-9299.
39. Heppner F.L., Musahl C., Arrighi I., Klein M.A., Rulicke T., Oesch B., et al. Prevention of scrapie pathogenesis by transgenic expression of anti-prion protein antibodies. Science. 294:2001;178-182.
40. Zulianello L., Kanako K., Scott M., Erpel S., Han D., Cohen F.E., Prusiner S.B. Dominant-negative inhibition of prion formation diminished by deletion mutagenesis of the prion protein. J. Virol. 74:2000;4351-4360.
41. Li R., Liu T., Wong B.-S., Pan T., Morillas M., Swietnicki W., et al. Identification of an epitope in the C terminus of normal prion protein whose expression is modulated by binding events in the N terminus. J. Mol. Biol. 301:2000;567-573.
42. Quaglio E., Chiesa R., Harris D.A. Copper converts the cellular prion protein into a protease-resistant species that is distinct from the scrapie isoform. J. Biol. Chem. 276:2001;11432-11438.
43. Qin, K., Yang, D. -S., Yang, Y., Chishti, A., Meng, L.-J., Kretzschmar, H. A. et al. J. Biol. Chem., 275, 19121-19131.
44. Harris D.A., Huber M.T., van Dijken P., Shyng S.-L., Chait B.T., Wang R. Processing of a cellular prion protein: identification of N- and C-terminal cleavage sites. Biochemistry. 32:1993;1009-1016.
45. Chen S.G., teplow D.B., Parchi P., Teller J.K., Gambetti P., Autilio-Gambetti L. Truncated forms of the human prion protein in normal brain and in prion diseases. J. Biol. Chem. 270:1995;19173-19180.
46. Mishra R.S., Gu Y., Bose S., Verghese S., Kalepu S., Singh N. Cell surface accumulation of a truncated transmembrane prion protein in GSS P102L. J. Biol. Chem. 277:2002;24554-24561.
47. Warner R.G., Hundt C., Weiss S., Turnbull J.E. Identification of the heparan sulfate binding sites in the cellular prion protein. J. Biol. Chem. 277:2002;18421-18430.
48. C helix 1 in the hydrophilic seeding of prion aggregates. Proc. Natl Acad. Sci. USA. 96:1999;11293-11298.
49. Vorberg I., Chan K., Priola S.A. Deletion of beta-strand and alpha-helix secondary structure in normal prion protein inhibits formation of its protease-resistant isoform. J. Virol. 75:2001;10024-10032.
50. Kascak R.J., Rubenstein R., Merz P.A., Tonna-DeMasi M., Fersko R., Carp R.I., et al. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril protein. J. Virol. 61:1987;3688-3693.
51. Barry R., Prusiner S.B. Monoclonal antibodies to the cellular and scrapie prion proteins. J. Infect. Dis. 154:1986;518-521.
52. Barbas C.F., Burton D.R., Scott J.K., Silverman G.J. Phage Display: A Laboratory Manual. 2001;Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
53. Williamson R.A., Peretz D., Smorodinsky N., Bastidas R., Serban H., Mehlhorn I., et al. Circumventing tolerance to generate autologous monoclonal antibodies to the prion protein. Proc. Natl Acad. Sci. USA. 93:1996;7279-7282.
54. Blochberger T.C., Cooper C., Peretz D., Tatzelt J., Griffith O.H., Baldwin M.A., Prusiner S.B. Prion protein expression in Chinese hamster ovary cells using a glutamine synthetase selection and amplification system. Protein Eng. 10:1997;1465-1473.