Monitoring plasma processing steps with a sensitive Western blot assay for the detection of the prion protein

Journal of Virological Methods

Volumn 84, Issue 1, 2000, Pages 77-89

  Lee, Douglas C ^a   Stenland, Christopher J ^a   Hartwell, Randal C ^a   Ford, Elizabeth K ^a   Cai, Kang ^a   Miller, Jeanette L C ^a   Gilligan, Kevin J ^a   Rubenstein, Richard ^b   Fournel, Michael ^a   Petteway Jr , Stephen R ^a  

^a BAYER CORPORATION   (United States)

^b NEW YORK STATE INSTITUTE FOR BASIC RESEARCH IN DEVELOPMENTAL DISABILITIES   (United States)

Author keywords

Prion protein; Transmissible spongiform encephalopathy; Western blot assay

Indexed keywords

PRION PROTEIN;

ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; CRYOPRECIPITATION; DISEASE ACTIVITY; DISEASE TRANSMISSION; IMMUNOBLOTTING; MOUSE; NONHUMAN; PRION DISEASE; PRIORITY JOURNAL; PROTEIN DETERMINATION; REPRODUCIBILITY; VIRUS DETECTION; VIRUS INFECTIVITY;

AMINO ACID SEQUENCE; ANIMALS; BIOLOGICAL ASSAY; BLOTTING, WESTERN; BRAIN CHEMISTRY; CRICETINAE; EPITOPES; FREEZING; HUMANS; PRECIPITATION; PRION DISEASES; PRIONS; PRPSC PROTEINS; SENSITIVITY AND SPECIFICITY; VIROLOGY;

ANIMALIA; RODENTIA;

EID: 0033991241     PISSN: 01660934     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0166-0934(99)00135-4     Document Type: Article

References (40)

1. Bolton D.C., McKinley M.P., Prusiner S.B. Molecular characteristics of the major scrapie prion protein. Biochemistry. 23:1984;5898-5906.
2. Brown P., Rohwer R.G., Dunstan B.C., MacAuley C., Gajdusek D.C., Drohan W.N. The distribution of infectivity in blood components and plasma derivatives in experimental models of transmissible spongiform encephalopathy. Transfusion. 38:1998;810-816.
3. Bueler H., Aguzzi A., Sailer A., Greiner R.-A., Autenried P., Aguet M., Weissmann C. Mice devoid of PrP are resistant to scrapie. Cell. 73:1993;1339-1347.
4. Ceroni M., Piccardo P., Safar J., Gadjusek D.C., Jr C.J.G. Scrapie infectivity and prion protein are distributed in the same pH range in agaraose isoelectric focusing. Neurology. 40:1990;508-513.
5. Darling A. Considerations in performing virus spiking experiments and process validation studies. Dev. Biol. Stand. 81:1993;221-229.
6. Diringer H. Sustained viremia in experimental hamster scrapie. Arch. Virol. 82:1984;105-109.
7. Dougherty R.M. Animal virus titration techniques. Harris R.J.C. Techniques in Experimental Virology. 1964;169-223 Academic Press, New York.
8. Gabizon R., McKinley M., Prusiner S. Purified prion proteins and scrapie infectivity copartition into liposomes. Proc. Natl. Acad. Sci. USA. 84(12):1987;4017-4021.
9. Golker C.F., Whiteman M.D., Gugel K.H., Gilles R., Stadler P., Kovatch R.M., Lister D., Wisher M.H., Calcagni C., Hubner G.E. Reduction of the infectivity of scrapie agent as a model for BSE in the manufacturing process of trasylol. Biologicals. 24:1996;103-111.
10. Grathwohl K.-U.D., Horiuchi M., Ishiguro N., Shinagawa M. Improvement of PrPSc detection in mouse spleen early at the preclinical stage of scrapie with collagenase-completed tissue homogenization and sarkosyl-NaCl extraction of PrPSc. Arch. Virol. 141:1996;1863-1874.
11. Grathwohl K.-U., Horiuchi M., Ishiguro N., Shinagawa M. Sensitive enzyme-linked immunoabsorbent assay for detection of PrPSc in crude extracts from scrapie-affected mice. J. Virol. Methods. 64:1997;205-216.
12. Kascsak R., Rubenstein R., Merz P.A., Tonna-DeMasi M., Fersko R., Carp R.I., Wisniewski H.M., Diringer H. Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J. Virol. 61(12):1987;3688-3693.
13. Kascsak R.J., Fersko R., Pulgiano D., Rubenstein R., Carp R.I. Immunodiagnosis of prion disease. Immunol. Invest. 26(1 and 2):1997;259-268.
14. Kimberlin R., Walker C.A., Fraser H. The genomic identity of different strains of mouse scrapie is expressed in hamsters and preserved on reisolation in mice. J. Virol. 70:1989;2017-2025.
15. Kuroda Y., Jr C.J.G., Amyx H.L., Gajusek D.C. Creutzfeldt-Jakob disease in mice: persistent viremia and preferential replication of virus in low-density lymphocytes. Infect. Immun. 41(1):1983;154-161.
16. Lasmezas C.I., Deslys J.-P., Robain O., Jargly A., Beringue V., Peyrin J.-M., Fournier J.-G., Hauw J.-J., Rossier J., Dormont D. Transmission of the BSE agent to mice in the absence of detectable abnormal prion protein. Science. 275:1997;402-405.
17. Manuelidis L., Fritch W. Infectivity and host responses in Creutzfeldt-Jakob disease. Virology. 216(1):1996;46-59.
18. Manuelidis E.E., Gorgacz E.J., Manelidis L. Viremia in experimental Cruetzfeldt-Jakob disease. Science. 200:1978;1069-1071.
19. Marsh R.F., Dees C., Castle B.E., Wade W.F., German T.L. Purification of the scrapie agent by density gradient centrifugation. J. Gen. Virol. 65:1984;415-421.
20. McKinley M.P., Bolton D.C., Prusiner S.B. A protease-resistant protein is a structural component of the scrapie prion. Cell. 35(1):1983;57-62.
21. Meyer R.K., McKinley M.P., Bowman K.A., Braunfield M.B., Barry R.A., Prusiner S.B. Separation and properties of cellular and scrapie prion proteins. Proc. Natl. Acad. Sci. USA. 83:1986;2310-2314.
22. O'Rourke K.I., Baszler T.V., Parish S.M., Knowles D.P. Preclinical detection of PrPsc in nictitating membrane lymphoid tissue of sheep. Vet. Rec. 142:1998;489-491.
23. Pan K.-M., Baldwin M., Nguyen J., Gasset M., Serban A., Groth D., Mehlhorn I., Huang Z., Fletterick R.J., Cohen F.E., Prusiner S.B. Conversion of alpha-helix into beta-sheets features in the formation of the scrapie prion protein. Proc. Natl. Acad. Sci. USA. 90:1993;10962-10966.
24. Pocchiari M., Peano S., Conz A., Eshkol A., Maillard F., Brown P., Gibbs C.J., Xi Y.G., Tenham-Fisher E., Macchi G. Combination ultrafiltration and 6 M urea treatment of human growth hormone effectively minimizes risk from potential Creutzfeldt-Jacobs disease virus contamination. Horm. Res. 35:1991;161-166.
25. Prusiner S.B. Novel proteinaceous infectious particles cause scrapie. Science. 216:1982;136-144.
26. Prusiner S. Genetic and infectious prion diseases. Arch. Neurol. 50:1993;1129-1153.
27. Prusiner S. Prion encephalopathies of animals and humans. Dev. Biol. Stand. 80:1993;31-44.
28. Prusiner S.B. The prion diseases. Brain Pathol. 8:1998;499-513.
29. Prusiner S.B. Prions. Proc. Natl. Acad. Sci. USA. 95:1998;13363-13383.
30. Rubenstein R., Carp R.I., Ju W., Scalici C., Papini M., Rubenstein A., Kascsak R. Concentration and distribution of infectivity and PrPsc following partial denaturation of a mouse-adapted and a hamster-adapted scrapie strain. Arch. Virol. 139:1994;301-311.
31. Safar, J., Ceroni, M., Piccardo, P., Liberski, P.P., Miyazaki, M., Gajdusek, D.C. and C.J. Gibbs, J. (1990) Subcellular Distribution and Physiochemical Properties of Scrapie-Associated Precursor Protein and Relationship with Scrapie Agent, Neurology 40, 503-508.
32. Safar J., Roller P.P., Gajdusek D.C., Gibbs C.J. Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J. Biol. Chem. 268(27):1993;20276-20284.
33. Safar J., Wille H., Itri V., Groth D., Serban H., Torchia M., Cohen F., Prusiner S. Eight prion strains have PrPSc molecules with different conformations. Nat. Med. 4(10):1998;1157-1165.
34. Serban D., Taraboulos A., DeArmond S.J., Prusiner S. Rapid detection of Creutzfeldt-Jakob disease and scrapie prion protein. Neurology. 40:1990;110-117.
35. Somerville R.A., Carp R.I. Altered scrapie infectivity estimates by titration and incubation period in the presence of detergents. Virology. 64:1983;2045-2050.
36. Sternberg J.C. A rate nephelometer for measuring specific proteins by immunoprecipitin reactions. Clin. Chem. 23:1977;1456-1464.
37. Taylor D.M. Inactivation of BSE agent. Dev. Biol. Stand. 75:1990;97-102.
38. Taylor D.M. Inactivation of SE agents. Br. Med. Bull. 49(4):1993;810-821.
39. Vandersande J. Current approaches to the preparation of plasma fractions. Goldstein J. Biotechnology of Blood. 1991;165-176 Butterworth-Heinemann, Boston, MA.
40. Will R., Ironside J., Cousens S., Estibeiro K., Alperovitch A., Poser S., Pocchiari M., Hofman A., Smith P. A new variant of Creutzfeldt-Jakob disease in the UK. Lancet. 347:1996;921-925.