A solid-phase assay for identification of modulators of prion protein interactions

Analytical Biochemistry

Volumn 323, Issue 1, 2003, Pages 54-64

  Maxson, Laura ^a,b   Wong, Cai'ne ^a,c   Herrmann, Lynn M ^a,d   Caughey, Byron ^a   Baron, Gerald S ^a  

^a NATIONAL INSTITUTES OF HEALTH   (United States)

^b YALE UNIVERSITY   (United States)

^c IDEXX LABORATORIES   (United States)

^d AGRICULTURAL RESEARCH SERVICE   (United States)

Author keywords

Anti TSE; Biotin; Cell free conversion; Prion; PrP; Solid phase assay

Indexed keywords

MODULATORS;

ANTI-TSE; BIOTIN; CELL-FREE; PRION; SOLID-PHASE;

PROTEINS;

ISOPROTEIN; PHTHALOCYANINE DERIVATIVE; PHTHALOCYANINE TETRASULFONATE; PRION PROTEIN; PROTEINASE; UNCLASSIFIED DRUG;

ANIMAL TISSUE; ARTICLE; BIOTINYLATION; CONTROLLED STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DETERMINATION; PROTEIN PROTEIN INTERACTION; REACTION ANALYSIS; SOLID;

ANIMALIA;

EID: 0242438133     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ab.2003.07.028     Document Type: Article

References (32)

1. McBride P.A., Bruce M.E., Fraser H. Immunostaining of scrapie cerebral amyloid plaques with antisera raised to scrapie-associated fibrils (SAF). Neuropathol. Appl. Neurobiol. 14:1988;325-336.
2. Brandner S., Isenmann S., Raeber A., Fischer M., Sailer A., Kobayashi Y., Marino S., Weissmann C., Aguzzi A. Normal host prion protein necessary for scrapie-induced neurotoxicity. Nature. 379:1996;339-343.
3. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA. 95:1998;13363-13383.
4. Kocisko D.A., Come J.H., Priola S.A., Chesebro B., Raymond G.J., Lansbury P.T. Jr., Caughey B. Cell-free formation of protease-resistant prion protein. Nature. 370:1994;471-474.
5. Hill A.F., Antoniou M., Collinge J. Protease-resistant prion protein produced in vitro lacks detectable infectivity. J. Gen. Virol. 80:1999;11-14.
6. Caughey B., Raymond G.J., Callahan M.A., Wong C., Baron G.S., Xiong L.W. Interactions and conversions of prion protein isoforms. Adv. Protein Chem. 57:2001;139-169.
7. Priola S.A., Raines A., Caughey W.S. Porphyrin and phthalocyanine antiscrapie compounds. Science. 287:2000;1503-1506.
8. Caughey W.S., Raymond L.D., Horiuchi M., Caughey B. Inhibition of protease-resistant prion protein formation by porphyrins and phthalocyanines. Proc. Natl. Acad. Sci. USA. 95:1998;12117-12122.
9. Ingrosso L., Ladogana A., Pocchiari M. Congo red prolongs the incubation period in scrapie-infected hamsters. J. Virol. 69:1995;506-508.
10. Caughey B., Race R.E. Potent inhibition of scrapie-associated PrP accumulation by congo red. J. Neurochem. 59:1992;768-771.
11. Demaimay R., Harper J., Gordon H., Weaver D., Chesebro B., Caughey B. Structural aspects of Congo red as an inhibitor of protease-resistant prion protein formation. J. Neurochem. 71:1998;2534-2541.
12. Horiuchi M., Baron G.S., Xiong L., Caughey B. Inhibition of interactions and interconversions of prion protein isoforms by peptide fragments from the C-terminal folded domain. J. Biol. Chem. 276:2001;15489-15497.
13. Bessen R.A., Raymond G.J., Caughey B. In situ formation of protease-resistant prion protein in transmissible spongiform encephalopathy-infected brain slices. J. Biol. Chem. 272:1997;15227-15231.
14. Bruce M.E., Will R.G., Ironside J.W., McConnell I., Drummond D., Suttie A., McCardle L., Chree A., Hope J., Birkett C., Cousens S., Fraser H., Bostock C.J. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature. 389:1997;498-501.
15. Hill A.F., Desbruslais M., Joiner S., Sidle K.C., Gowland I., Collinge J., Doey L.J., Lantos P. The same prion strain causes vCJD and BSE. Nature. 389:1997;448-450.
16. Horiuchi M., Chabry J., Caughey B. Specific binding of normal prion protein to the scrapie form via a localized domain initiates its conversion to the protease-resistant state. EMBO J. 18:1999;3193-3203.
17. Sc-dependent cell-free formation of protease-resistant prion protein. EMBO J. 20:2001;377-386.
18. Caughey B., Raymond G.J., Ernst D., Race R.E. N-terminal truncation of the scrapie-associated form of PrP by lysosomal protease(s): implications regarding the site of conversion of PrP to the protease-resistant state. J. Virol. 65:1991;6597-6603.
19. Sc) into contiguous membranes. EMBO J. 21:2002;1031-1040.
20. Raymond G.J., Hope J., Kocisko D.A., Priola S.A., Raymond L.D., Bossers A., Ironside J., Will R.G., Chen S.G., Petersen R.B., Gambetti P., Rubenstein R., Smits M.A., Lansbury P.T. Jr., Caughey B. Molecular assessment of the potential transmissibilities of BSE and scrapie to humans. Nature. 388:1997;285-288.
21. DebBurman S.K., Raymond G.J., Caughey B., Lindquist S. Chaperone-supervised conversion of prion protein to its protease-resistant form. Proc. Natl. Acad. Sci. USA. 94:1997;13938-13943.
22. Morillas M., Swietnicki W., Gambetti P., Surewicz W.K. Membrane environment alters the conformational structure of the recombinant human prion protein. J. Biol. Chem. 274:1999;36859-36865.
23. Sanghera N., Pinheiro T.J. Binding of prion protein to lipid membranes and implications for prion conversion. J. Mol. Biol. 315:2002;1241-1256.
24. Baron G.S., Caughey B. Effect of GPI anchor-dependent and -independent prion protein association with model raft membranes on conversion to the protease-resistant isoform. J. Biol. Chem. 278:2003;14883-14892.
25. Berthelier V., Hamilton J.B., Chen S., Wetzel R. A microtiter plate assay for polyglutamine aggregate extension. Anal. Biochem. 295:2001;227-236.
26. 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.
27. 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.
28. Peretz D., Williamson R.A., Matsunaga Y., Serban H., Pinilla C., Bastidas R.B., Rozenshteyn R., James T.L., Houghten R.A., Cohen F.E., Prusiner S.B., Burton D.R. 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.
29. Gabizon R., Meiner Z., Halimi M., Ben-Sasson S.A. Heparin-like molecules bind differentially to prion proteins and change their intracellular metabolic fate. J. Cell Physiol. 157:1993;319-325.
30. Caughey B., Brown K., Raymond G.J., Katzenstein G.E., Thresher W. Binding of the protease-sensitive form of PrP (prion protein) to sulfated glycosaminoglycan and congo red. J. Virol. 68:1994;2135-2141.
31. Priola S.A., Lawson V.A. Glycosylation influences cross-species formation of protease-resistant prion protein. EMBO J. 20:2001;6692-6699.
32. Kocisko D.A., Barton G.S., Rubenstein R., Chen J., Kuizon S., Caughey B. New inhibitors of scrapie-associated prion protein formation in a library of 2000 drugs and natural products. J. Virol. 77:2003;10288-10294.