Novel antibody-lectin enzyme-linked immunosorbent assay that distinguishes prion proteins in sporadic and variant cases of Creutzfeldt-Jakob disease

Journal of Clinical Microbiology

Volumn 43, Issue 3, 2005, Pages 1118-1126

  Pan, Tao ^c   Li, Ruliang ^a   Wong, Boon Seng ^a   Kang, Shin Chung ^a   Ironside, James ^b   Sy, Man Sun ^a  

^a CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF EDINBURGH   (United Kingdom)

^c Biomedical Research Building ^*

Author keywords

[No Author keywords available]

Indexed keywords

AGGLUTININ; CONCANAVALIN A; GLYCAN; LECTIN; PLANT LECTIN; PRION PROTEIN; PROTEINASE K; RICINUS COMMUNIS EXTRACT;

ARTICLE; BINDING AFFINITY; CONTROLLED STUDY; CREUTZFELDT JAKOB DISEASE; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; HUMAN TISSUE; IMMUNOREACTIVITY; NONHUMAN; PHENOTYPE; PRIORITY JOURNAL;

BIOTINYLATION; CREUTZFELDT-JAKOB SYNDROME; DIAGNOSIS, DIFFERENTIAL; ENDOPEPTIDASE K; ENZYME-LINKED IMMUNOSORBENT ASSAY; HUMANS; PLANT LECTINS; POLYSACCHARIDES; PRIONS;

ALEURIA AURANTIA; RICINUS COMMUNIS;

EID: 14944345146     PISSN: 00951137     EISSN: None     Source Type: Journal    
DOI: 10.1128/JCM.43.3.1118-1126.2005     Document Type: Article

References (32)

1. Bolton, D. C., M. P. McKinley, and S. B. Prusiner. 1982. Identification of a protein that purifies with the scrapie prion. Science 218:1309-1311.
2. Bruce, M., H. Fraser, P. Mcbride, J. Scott, and A. Dickinson. 1992. The basis of strain variations in scrapie, p. 497-508. In S. B. Prusiner (ed.), Prion diseases in humans and animals. Ellis Horwood, London, United Kingdom.
3. DeArmond, S. J., Y. Qiu, H. Sanchez, P. R. Spilman, A. Ninchak-Casey, D. Alonso, and V. Daggett. 1999. PrPc glycoform heterogeneity as a function of brain region: implications for selective targeting of neurons by prion strains. J. Neuropathol. Exp. Neurol. 58:1000-1009.
4. Endo, T., D. Groth, S. B. Prusiner, and A. Kobata. 1989. Diversity of oligosaccharide structures linked to asparagines of the scrapie prion protein. Biochemistry 28:8380-8388.
5. 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.
6. Haraguchi, T., S. Fisher, S. Olofsson, T. Endo, D. Groth, A. Tarentino, D. R. Borchelt, D. Teplow, L. Hood, A. Burlingame, et al. 1989. Asparagine-linked glycosylation of the scrapie and cellular prion proteins. Arch. Biochem. Biophys. 274:1-13.
7. Hecker, R., A. Taraboulos, M. Scott, K. M. Pan, S. L. Yang, M. Torchia, K. Jendroska, S. J. DeArmond, and S. B. Prusiner. 1992. Replication of distinct scrapie prion isolates is region specific in brains of transgenic mice and hamsters. Genes Dev. 6:1213-1228.
8. Hill, A. F., S. Joiner, J. D. Wadsworth, K. C. Sidle, J. E. Bell, H. Budka, J. W. Ironside, and J. Collinge. 2003. Molecular classification of sporadic Creutzfeldt-Jakob disease. Brain 126:1333-1346.
9. Lehmann, S., and D. A. Harris. 1997. Blockade of glycosylation promotes acquisition of scrapie-like properties by the prion protein in cultured cells. J. Biol. Chem. 272:21479-21487. (Erratum, 273:5988, 1998.)
10. Li, R., T. Liu, B.-S. Wong, T. Pan, M. Morillas, W. Swetnicki, K. O'Rourke, P. Gamhetti, W. K. Surewicz, and M.-S. Sy. 2000. 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. 301:567-574.
11. Liu, T., T. Zwingman, R. Li, T. Pan, B. S. Wong, R. B. Petersen, P. Gambetti, K. Herrup, and M.-S. Sy. 2001. Differential expression of cellular prion protein in mouse brain as detected with multiple anti-PrP monoclonal antibodies. Brain Res. 896:118-129.
12. Manuelidis, L., S. Valley, and E. E. Manuelidis. 1985. Specific proteins associated with Creutzfeldt-Jakob disease and scrapie share antigenic and carbohydrate determinants. Proc. Natl. Acad. Sci. USA 82:4263-4267.
13. Oesch, B., D. Westaway, M. Walchli, M. P. McKinley, S. B. Kent, R. Aebersold, R. A. Barry, P. Tempst, D. B. Teplow, and L. E. Hood. 1985. A cellular gene encodes scrapie PrP 27-30 protein. Cell 40:735-746.
14. 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 alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 90:10962-10966.
15. Pan, T., M. Colucci, B. S. Wong, R. Li, T. Liu, R. B. Petersen, S. Chen, P. Gambetti, and M.-S. Sy. 2001. Novel differences between two human prion strains revealed by two-dimensional gel electrophoresis. J. Biol. Chem. 276: 37284-37288.
16. Pan, T., R. Li, B. S. Wong, T. Liu, P. Gambetti, and M.-S. Sy. 2002. Heterogeneity of normal prion protein in two-dimensional immunoblot: presence of various glycosylated and truncated forms. J. Neurochem. 81:1092-1101.
17. Pan, T., B. S. Wong, T. Liu, R. Li, R. B. Petersen, and M.-S. Sy. 2002. Cell-surface prion protein interacts with glycosaminoglycans. Biochem. J. 368:81-90.
18. Parchi, P., R. Castellani, S. Capellari, B. Ghetti, K. Young, S. G. Chen, M. Farlow, D. W. Dickson, A. A. Sima, J. Q. Trojanowski, R. B. Petersen, and P. Gambetti. 1996. Molecular basis of phenotypic variability in sporadic Creutzfeldt-Jakob disease. Ann. Neurol. 39:767-778.
19. Parchi, P., A. Giese, S. Capellari, P. Brown, W. Schulz-Schaeffer, O. Windl, I. Zerr, H. Budka, N. Kopp, P. Piccardo, S. Poser, A. Rojiani, N. Streichemberger, J. Julien, C. Vital, B. Ghetti, P. Gambetti, and H. Kretzschmar. 1999. Classification of sporadic Creutzfeldt-Jakob disease based on molecular and phenotypic analysis of 300 subjects. Ann. Neurol. 46:224-233.
20. Peretz, D., M. R. Scott, D. Groth, R. A. Williamson, D. R. Burton, F. E. Cohen, and S. B. Prusiner. 2001. Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci. 10:854-863.
21. Prusiner, S. B. 1982. Novel proteinaceous infectious particles cause scrapie. Science 216:136-144.
22. Prusiner, S. B. 1998. Prions. Proc. Natl. Acad. Sci. USA 95:13363-13383.
23. 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.
24. Rogers, M., A. Taraboulos, M. Scott, D. Groth, and S. B. Prusiner. 1990. Intracellular accumulation of the cellular prion protein after mutagenesis of its Asn-linked glycosylation sites. Glycobiology 1:101-109.
25. Rudd, P. M., T. Endo, C. Colominas, D. Groth, S. F. Wheeler, D. J. Harvey, M. R. Wormald, H. Serban, S. B. Prusiner, A. Kobata, and R. A. Dwek. 1999. Glycosylation differences between the normal and pathogenic prion protein isoforms. Proc. Natl. Acad. Sci. USA 96:13044-13049.
26. Safar, J. 1990. Scrapie isoform of scrapie-associated protein. J. Am. Vet. Med. Assoc. 196:1681.
27. Safar, J., F. E. Cohen, and S. B. Prusiner. 2000. Quantitative traits of prion strains are enciphered in the conformation of the prion protein. Arch. Virol. Suppl. 16:227-235.
28. Somerville, R. A., and L. A. Ritchie. 1990. Differential glycosylation of the protein (PrP) forming scrapie-associated fibrils. J. Gen. Virol. 71:833-839.
29. Stahl, N., M. A. Baldwin, D. B. Teplow, L. Hood, B. W. Gibson, A. L. Burlingame, and S. B. Prusiner. 1993. Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32:1991-2002.
30. Stimson, E., J. Hope, A. Chong, and A. L. Burlingame. 1999. Site-specific characterization of the N-linked glycans of murine prion protein by high-performance liquid chromatography/electrospray mass spectrometry and exoglycosidase digestions. Biochemistry 38:4885-4895.
31. Winklhofer, K. F., U. Heller, A. Reintjes, and J. Tatzelt. 2003 Inhibition of complex glycosylation increases the formation of PrPsc. Traffic 4:313-322.
32. Zanusso, G., D. Liu, S. Ferrari, I. Hegyi, X. Yin, A. Aguzzi, S. Hornemann, S. Liemann, R. Glockshuber, J. C. Manson, P. Brown, R. B. Petersen, P. Gambetti, and M.-S. Sy. 1998. Prion protein expression in different species: analysis with a panel of new mAbs. Proc Natl Acad Sci USA 95:8812-8816.