Mapping the prion protein using recombinant antibodies

Journal of Virology

Volumn 72, Issue 11, 1998, Pages 9413-9418

  Williamson, R Anthony ^a   Peretz, David ^b   Pinilla, Clemencia ^c   Ball, Hadyn ^b   Bastidas, Raiza B ^a   Rozenshteyn, Roman ^a   Houghten, Richard A ^c   Prusiner, Stanley B ^b   Burton, Dennis R ^a  

^a SCRIPPS RESEARCH INSTITUTE   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c TORREY PINES INSTITUTE FOR MOLECULAR STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODY; PRION PROTEIN; RECOMBINANT PROTEIN;

ANIMAL EXPERIMENT; ANTIGEN RECOGNITION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; EPITOPE MAPPING; MOUSE; NONHUMAN; PEPTIDE MAPPING; PRION DISEASE; PRIORITY JOURNAL; PROTEIN DETERMINATION; PROTEIN PROCESSING;

EID: 0031710237     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.72.11.9413-9418.1998     Document Type: Article

References (35)

1. Barbas, C. F., and R. A. Lerner. 1991. Combinatorial immunoglobulin libraries on the surface of phage (Phabs): rapid selection of antigen-specific Fabs, p. 119-124. In R. A. Lerner and D. R. Burton (ed.), Methods: a companion to methods in enzymology. Academic Press, Orlando, Fla.
2. Barry, R. A., and S. B. Prusiner. 1986. Monoclonal antibodies to the cellular and scrapie prion proteins. J. Infect. Dis. 154:518-521.
3. Borchelt, D. R., M. Scott, A. Taraboulos, N. Stahl, and S. B. Prusiner. 1990. Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells. J. Cell Biol. 110:743-752.
4. Büeler, H., M. Fischer, Y. Lang, H. Bluethmann, H. P. Lipp, S. J. DeArmond, S. B. Prusiner, M. Aguet, and C. Weissmann. 1992. Normal development and behaviour of mice lacking the neuronal cell-surface PrP protein. Nature 356:577-582.
5. Burton, D. R., and C. F. Barbas. 1994. Human antibodies from combinatorial libraries. Adv. Immunol. 57:191-280.
6. Caughey, B. W., and G. J. Raymond. 1991. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease- and phospholipase-sensitive. J. Biol. Chem. 266:18217-18223.
7. Ditzel, H. J., J. M. Binley, J. P. Moore, J. Sodroski, N. Sullivan, L. S. W. Sawyer, R. M. Hendry, W.-P. Yang, C. F. Barbas, and D. R. Burton. 1995. Neutralizing recombinant human antibodies to a conformational V2- and CD4-binding site-sensitive epitope of HIV-1 gp120 isolated by using an epitope-masking procedure. J. Immunol. 154:893-906.
8. Donne, D. G., J. H. Viles, D. Groth, I. Mehlhorn, T. L. James, F. E. Cohen, S. B. Prusiner, P. E. Wright, and H. J. Dyson. 1997. Structure of the recombinant ful-length hamster prion protein PrP(29-231): the N-terminus is highly flexible. Proc. Natl. Acad. Sci. USA 94:13452-13457.
9. Gabizon, R., M. P. McKinley, and S. B. Prusiner. 1987. Purified prion proteins and scrapie infectivity copartition into liposomes. Proc. Natl. Acad. Sci. USA 84:4017-4021.
10. Gabizon, R., and S. B. Prusiner. 1990. Prion liposomes. Biochem. J. 266:1-14.
11. Gasset, M., M. A. Baldwin, R. J. Fletterick, and S. B. Prusiner. 1993. Perturbation of the secondary structure of the scrapie prion protein under conditions that alter infectivity. Proc. Natl. Acad. Sci. USA 90:1-5.
12. Huse, W. D., L. Sastry, S. A. Iverson, A. S. Kang, M. Alting-Mees, D. R. Burton, S. J. Benkovic, and R. A. Lerner. 1989. Generation of a large combinatorial library of the immunoglobulin repertoire in phage lambda. Science 246:1275-1281.
13. James, T. L., H. Liu, N. B. Ulyanov, S. Farr-Jones, H. Zhang, D. Donne, K. Kaneko, D. Groth, I. Mehlhorn, F. E. Cohen, and S. B. Prusiner. 1997. Solution structure of a 142-residue recombinant prion protein corresponding to the infectious fragment of the scrapie isoform. Proc. Natl. Acad. Sci. USA 94:10086-10091.
14. Kaneko, K., D. Peretz, K.-M. Pan, T. C. Blochberger, H. Wille, R. Gabizon, O. H. Griffith, F. E. Cohen, M. A. Baldwin, and S. B. Prusiner. 1995. Prion protein (PrP) synthetic peptides induce cellular PrP to acquire properties of the scrapie isoform. Proc. Natl. Acad. Sci. USA 92:11160-11164.
15. Kascsak, R. J., R. Rubenstein, P. A. Merz, M. Tonna-DeMasi, R. Fersko, R. I. Carp, H. M. Wisniewski, and H. Diringer. 1987. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61:3688-3693.
16. Klebe, R. J., and F. H. Ruddle. 1969. Neuroblastoma: cell culture analysis of a differentiating stem cell system. J. Cell Biol. 43:69a.
17. Masters, C. L., D. C. Gajdusek, and C. J. Gibbs, Jr. 1981. Creutzfeldt-Jakob disease virus isolations from the Gerstmann-Straussler syndrome with an analysis of the various forms of amyloid plaque deposition in the virus-induced spongiform encephalopathies. Brain 104:559-588.
18. McKinley, M. P., R. K. Meyer, L. Kenaga, F. Rahbar, R. Cotter, A. Serban, and S. B. Prusiner. 1991. Scrapie prion rod formation in vitro requires both detergent extraction and limited proteolysis. J. Virol. 65:1340-1351.
19. Mehlhorn, I., D. Groth, J. Stockel, B. Moffat, D. Reilly, D. Yansura, W. S. Willet, M. Baldwin, R. Fletterick, F. E. Cohen, R. Vandlen, D. Henner, and S. B. Prusiner. 1996. High-level expression and characterization of a purified 142-residue polypeptide of the prion protein. Biochemistry 35:5528-5537.
20. Muramoto, T., M. Scott, F. E. Cohen, and S. B. Prusiner. 1997. Recombinant scrapie-like prion protein of 106 amino acids is soluble. Proc. Natl. Acad. Sci. USA 93:15457-15462.
21. Pan, K.-M., M. Baldwin, J. Nguyen, M. Gasset, A. Serban, D. Groth, I. Mehlhorn, Z. Huang, R. J. Fletterick, F. E. Cohen, and S. B. Prusiner. 1993. Conversion of α-helices into β-sheets features in the formation of the scrapie prion protein. Proc. Natl. Acad. Sci. USA 90:10926-10966.
22. Peretz, D., R. A. Williamson, Y. Matsunaga, H. Serban, C. Pinilla, R. Bastidas, R. Rozenshteyn, D. P. Papahadjopoulos, T. J. James, R. A. Houghten, F. E. Cohen, S. B. Prusiner, and D. R. Burton. 1997. A conformational transition at the N-terminus of the prion protein features in formation of the scrapie isoform. J. Mol. Biol. 273:614-622.
23. Petersen, G., D. Song, B. Hugle-Dorr, I. Oldenburg, and E. K. Bautz. 1995. Mapping of linear epitopes recognized by monoclonal antibodies with gene-fragment phage display libraries. Mol. Gen. Genet. 249:425-431.
24. Prusiner, S. B. 1996. Transgenetics of prion diseases. Curr. Top. Microbiol. Immunol. 206:275-304.
25. Prusiner, S. B. 1996. Molecular biology and pathogenesis of prion diseases. Trends Biochem. Sci. 21:482-487.
26. Prusiner, S. B., D. Groth, A. Serban, R. Koehler, D. Foster, M. Torchia, D. R. Burton, S.-L. Yang, and S. J. DeArmond. 1993. Ablation of the prion protein (PrP) gene in mice prevents scrapie and facilitates production of anti-PrP antibodies. Proc. Natl. Acad. Sci. USA 90:10608-10612.
27. Prusiner, S. B., M. P. McKinley, K. A. Bowman, D. C. Bolton, P. E. Bendheim, D. F. Groth, and G. G. Glenner. 1983. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35:349-358.
28. Riek, R., S. Hornemann, G. Wider, M. Billeter, R. Glockshuber, and K. Wuthrich. 1996. NMR structure of the mouse prion protein domain PrP (121-231). Nature 382:180-182.
29. Riek, R., S. Hornemann, G. Wider, R. Glockshuber, and K. Wuthrich. 1997. NMR characterization of the full-length recombinant murine prion protein, mPrP(23-231). FEBS Lett. 413:282-288.
30. Rogers, M., D. Serban, T. Gyuris, M. Scott, T. Torchia, and S. B. Prusiner. 1991. Epitope mapping of the Syrian hamster prion protein utilizing chimeric and mutant genes in a vaccinia virus expression system. J. Immunol. 147: 3568-3574.
31. Safar, J., P. P. Roller, D. C. Gajdusek, and C. J. Gibbs, Jr. 1993. Conformational transitions, dissociation and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268:20276-20284.
32. Taraboulos, A., K. Jendroska, D. Serban, S.-L. Yang, S. J. DeArmond, and S. B. Prusiner. 1992. Regional mapping of prion proteins in brain. Proc. Natl. Acad. Sci. USA 89:7620-7624.
33. Williamson, R. A., R. Burioni, P. P. Sanna, L. J. Partridge, C. F. Barbas, and D. R. Burton. 1993. Human monoclonal antibodies against a plethora of viral pathogens from single combinatorial libraries. Proc. Natl. Acad. Sci. USA 90: 4141-4145.
34. Williamson, R. A., D. Peretz, N. Smorodinsky, R. Bastidas, A. Serban, I. Mehlhorn, S. DeArmond, S. B. Prusiner, and D. R. Burton. 1996. Circumventing tolerance in order to generate autologous monoclonal antibodies to the prion protein. Proc. Natl. Acad. Sci. USA 93:7279-7282.
35. Zhang, H., K. Kaneko, J. T. Nguyen, T. L. Livshits, M. A. Baldwin, F. E. Cohen, T. L. James, and S. B. Prusiner. 1995. Conformational transitions in peptides containing two putative α-helices of the prion protein. J. Mol. Biol. 250:514-526.