Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins.

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J Virol. 1987 December; 61(12): 3688-3693

Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins.

R J Kascsak, R Rubenstein, P A Merz, M Tonna-DeMasi, R Fersko, R I Carp, H M Wisniewski and H Diringer

New York State Institute for Basic Research in Developmental Disabilities, Staten Island 10314.

ABSTRACT

Antibody response in mice to scrapie-associated fibril proteins(protease-resistant proteins [PrPs]) was generated to differentepitopes depending on the source of antigen. Mice respondeddifferently to PrPs isolated from scrapie-infected animals ofhomologous (mouse) versus heterologous (hamster) species. Anenzyme-linked immunosorbent assay established to monitor thisantibody response in mice immunized with PrPs was unable todetect such a response in scrapie-infected mice. A monoclonalantibody (MAb), 263K 3F4, derived from a mouse immunized withhamster 263K PrPs reacted with hamster but not mouse PrPs. MAb263K 3F4 also recognized normal host protein of 33 to 35 kilodaltonsin brain tissue from hamsters and humans but not from bovine,mouse, rat, sheep, or rabbit brains. This is the first demonstrationof epitope differences on this host protein in different species.The defining of various epitopes on PrP through the use of MAbswill lead to a better understanding of the relationship of PrPsto their host precursor protein and to the infectious scrapieagent.

J Virol. 1987 December; 61(12): 3688-3693

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Kneipp, J., Beekes, M., Lasch, P., Naumann, D. (2002). Molecular Changes of Preclinical Scrapie Can Be Detected by Infrared Spectroscopy. J. Neurosci. 22: 2989-2997 [Abstract] [Full Text]
Bosque, P. J., Ryou, C., Telling, G., Peretz, D., Legname, G., DeArmond, S. J., Prusiner, S. B. (2002). Prions in skeletal muscle. Proc. Natl. Acad. Sci. USA 99: 3812-3817 [Abstract] [Full Text]
Taratuto, A. L., Piccardo, P., Reich, E. G., Chen, S. G., Sevlever, G., Schultz, M., Luzzi, A. A., Rugiero, M., Abecasis, G., Endelman, M., Garcia, A. M., Capellari, S., Xie, Z., Lugaresi, E., Gambetti, P., Dlouhy, S. R., Ghetti, B. (2002). Insomnia associated with thalamic involvement in E200K Creutzfeldt-Jakob disease. Neurology 58: 362-367 [Abstract] [Full Text]
Mastrianni, J. A., Capellari, S., Telling, G. C., Han, D., Bosque, P., Prusiner, S. B., DeArmond, S. J. (2001). Inherited prion disease caused by the V210I mutation: Transmission to transgenic mice. Neurology 57: 2198-2205 [Abstract] [Full Text]
Vorberg, I., Chan, K., Priola, S. A. (2001). Deletion of {beta}-Strand and {alpha}-Helix Secondary Structure in Normal Prion Protein Inhibits Formation of Its Protease-Resistant Isoform. J. Virol. 75: 10024-10032 [Abstract] [Full Text]
Race, R., Raines, A., Raymond, G. J., Caughey, B., Chesebro, B. (2001). Long-Term Subclinical Carrier State Precedes Scrapie Replication and Adaptation in a Resistant Species: Analogies to Bovine Spongiform Encephalopathy and Variant Creutzfeldt-Jakob Disease in Humans. J. Virol. 75: 10106-10112 [Abstract] [Full Text]
McBride, P. A., Schulz-Schaeffer, W. J., Donaldson, M., Bruce, M., Diringer, H., Kretzschmar, H. A., Beekes, M. (2001). Early Spread of Scrapie from the Gastrointestinal Tract to the Central Nervous System Involves Autonomic Fibers of the Splanchnic and Vagus Nerves. J. Virol. 75: 9320-9327 [Abstract] [Full Text]
Shaked, Y., Rosenmann, H., Hijazi, N., Halimi, M., Gabizon, R. (2001). Copper Binding to the PrP Isoforms: a Putative Marker of Their Conformation and Function. J. Virol. 75: 7872-7874 [Abstract] [Full Text]
Piccardo, P., Liepnieks, J. J., William, A., Dlouhy, S. R., Farlow, M. R., Young, K., Nochlin, D., Bird, T. D., Nixon, R. R., Ball, M. J., DeCarli, C., Bugiani, O., Tagliavini, F., Benson, M. D., Ghetti, B. (2001). Prion Proteins with Different Conformations Accumulate in Gerstmann-Straussler-Scheinker Disease Caused by A117V and F198S Mutations. Am. J. Pathol. 158: 2201-2207 [Abstract] [Full Text]
Priola, S. A., Chabry, J., Chan, K. (2001). Efficient Conversion of Normal Prion Protein (PrP) by Abnormal Hamster PrP Is Determined by Homology at Amino Acid Residue 155. J. Virol. 75: 4673-4680 [Abstract] [Full Text]
Supattapone, S., Bouzamondo, E., Ball, H. L., Wille, H., Nguyen, H.-O. B., Cohen, F. E., DeArmond, S. J., Prusiner, S. B., Scott, M. (2001). A Protease-Resistant 61-Residue Prion Peptide Causes Neurodegeneration in Transgenic Mice. Mol. Cell. Biol. 21: 2608-2616 [Abstract] [Full Text]
Peretz, D., Scott, M. R., Groth, D., Williamson, R. A., Burton, D. R., Cohen, F. E., Prusiner, S. B. (2001). Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci. 10: 854-863 [Abstract] [Full Text]
Appel, T. R., Wolff, M., von Rheinbaben, F., Heinzel, M., Riesner, D. (2001). Heat stability of prion rods and recombinant prion protein in water, lipid and lipid-water mixtures. J. Gen. Virol. 82: 465-473 [Abstract] [Full Text]
Baron, T. G. M., Biacabe, A.-G. (2001). Molecular Analysis of the Abnormal Prion Protein during Coinfection of Mice by Bovine Spongiform Encephalopathy and a Scrapie Agent. J. Virol. 75: 107-114 [Abstract] [Full Text]
Supattapone, S., Nguyen, H.-O. B., Muramoto, T., Cohen, F. E., DeArmond, S. J., Prusiner, S. B., Scott, M. (2000). Affinity-Tagged Miniprion Derivatives Spontaneously Adopt Protease-Resistant Conformations. J. Virol. 74: 11928-11934 [Abstract] [Full Text]
Korth, C., Kaneko, K., Prusiner, S. B. (2000). Expression of unglycosylated mutated prion protein facilitates PrPSc formation in neuroblastoma cells infected with different prion strains. J. Gen. Virol. 81: 2555-2563 [Abstract] [Full Text]
Iniguez, V., McKenzie, D., Mirwald, J., Aiken, J. (2000). Strain-specific propagation of PrPSc properties into baculovirus-expressed hamster PrPC. J. Gen. Virol. 81: 2565-2571 [Abstract] [Full Text]
Parchi, P., Zou, W., Wang, W., Brown, P., Capellari, S., Ghetti, B., Kopp, N., Schulz-Schaeffer, W. J., Kretzschmar, H. A., Head, M. W., Ironside, J. W., Gambetti, P., Chen, S. G. (2000). Genetic influence on the structural variations of the abnormal prion protein. Proc. Natl. Acad. Sci. USA 97: 10168-10172 [Abstract] [Full Text]

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