Skip to main content
SpringerLink
Log in

Detection of species specific epitopes of mouse and hamster prion proteins (PrPs) by anti-peptide antibodies

  • Brief Report
  • Published:
Archives of Virology Aims and scope Submit manuscript

Summary

Antisera to four synthetic peptides containing the substitutions between mouse and hamster prion proteins (PrPs) were produced in rabbits. The synthetic peptides used represent two mouse (Mo-I: residues 100–115 and Mo-V: residues 199–208) and two hamster PrP subregion sequences (Ha-I: 101–116 and Ha-V: 200–209). All antisera reacted strongly with homologous peptides but either not at all or poorly with heterologous peptides in enzyme-linked immunosorbent assay (ELISA). Antisera to Mo-I and Mo-V recognized mouse PrPSc but not hamster PrPSc in western blot analysis (WB) and ELISA. Antisera to Ha-I contain antibodies specific to hamster PrPSc. The results indicate that these regions of PrPSc constitute species-specific epitopes. In contrast to these antisera, the antiserum to Ha-V recognized neither hamster nor mouse PrPSc. In this study, we identified mouse subregion-V as a species-specific epitope.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Log in via an institution

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Institutional subscriptions

References

  1. Basler K, Oesch B, Scott M, Westaway D, Wälchli M, Groth DF, McKinley MP, Prusiner SB, Weissmann C (1986) Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46: 417–428

    PubMed  Google Scholar 

  2. Bolton DC, Mckinley MP, Prusiner SB (1982) Identification of a protein that purifies with the scrapie prion. Science 218: 1309–1311

    PubMed  Google Scholar 

  3. Bolton DC, Seligman SJ, Bablanian G, Windsor D, Scala LJ, Kim KS, Chem C-MJ, Kascsak RJ, Bendheim PE (1991) Molecular location of a species-specific epitope on the hamster scrapie agent protein. J Virol 65: 3667–3675

    PubMed  Google Scholar 

  4. Bolton DC, Bendheim PE (1991) Purification of scrapie agents: how far have we come? In: Chesebro BW (ed) Transmissible spongiform encephalopathies: scrapie, BSE and related human disorders. Curr Top Microbiol Immunol 172: 39–55

    PubMed  Google Scholar 

  5. Büeler H, Aguzzi A, Sailer A, Greiner R-A, Autenried P, Aguet M, Weissmann C (1993) Mice devoid of PrP are resistant to scrapie. Cell 73: 1339–1347

    PubMed  Google Scholar 

  6. Gomi H, Yokoyama T, Fujimoto K, Ikeda T, Katoh A, Itoh T, Itohara S (1995) Mice devoid of the glial fibrillary acidic protein develop normally and are susceptible to scrapie prions. Neuron 14: 29–41

    PubMed  Google Scholar 

  7. Groschup MH, Langeveld J, Pfaff E (1994) The major species specific epitope in prion proteins of ruminants. Arch Virol 136: 423–431

    PubMed  Google Scholar 

  8. Hornbeck P (1991) Antibody detection and preparation. Curr Prot Immunol 1: 2.1.1–2.1.22

    Google Scholar 

  9. Kascsak RJ, Rubenstein R, Merz PA, Tonna-DeMasi M, Fersko R, Carp RI, Wisniewski HM, Diringer H (1987) Mouse polyclonal and monoclonal antibody to scrapie-associated fibril proteins. J Virol 61: 3688–3693

    PubMed  Google Scholar 

  10. Kimberlin RH (1991) Agent-host interactions and pathogenesis. Bradley R, Savey M, Marchant B (ed) In: Sub-acute spongiform encephalopathies: Proceedings of a seminar in the CEC agricultural research programme. Kluwer, Dordrecht, pp 137–147

    Google Scholar 

  11. Liao Y-CJ, Lebo RV, Clawson GA, Smuckler EA (1986) Human prion protein cDNA: molecular cloning, chromosomal mapping, and biological implications. Science 233: 364–367

    PubMed  Google Scholar 

  12. Locht C, Chesebro B, Race R, Keith JM (1986) Molecular cloning and complete sequence of prion protein cDNA from mouse brain infected with the scrapie agent. Proc Natl Acad Sci USA 83: 6372–6376

    PubMed  Google Scholar 

  13. Oesch B, Westaway D, Wälchli M, McKinley MP, Kent SBH, Aebersold R, Barry RA, Tempst P, Teplow DB, Hood LE, Prusiner SB, Weissmann C (1985) A cellular gene encodes scrapie PrP 27–30 protein. Cell 40: 735–746

    PubMed  Google Scholar 

  14. Pan K-M, Baldwin M, Nguyen J, Gasset M, Serban A, Groth D, Mehlhorn I, Huang Z, Fletterick RJ, Cohen FE, Prusiner SB (1993) Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90: 10962–10966

    PubMed  Google Scholar 

  15. Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE (1984) Purification and structural studies of a major scrapie prion protein. Cell 38: 127–134

    PubMed  Google Scholar 

  16. Prusiner SB, Scott M, Foster D, Pan K-M, Groth D, Mirenda C, Torchia M, Yang S-L, Serban D, Carlson GA, Hoppe PC, Westaway D, DeArmond SJ (1990) Transgenetic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 63: 673–686

    PubMed  Google Scholar 

  17. Prusiner SB, Groth D, Serban A, Koehler R, Foster D, Torchia M, Burton D, Yang S-L, DeArmond SJ (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

    PubMed  Google Scholar 

  18. Robakis NK, Sawh PR, Wolfe GC, Rubenstein R, Carp RI, Innis MA (1986) Isolation of a cDNA clone encoding the leader peptide of prion protein and expression of the homologous gene in various tissues. Proc Natl Acad Sci USA 83: 6377–6381

    PubMed  Google Scholar 

  19. Rogers M, Serban D, Gyuris T, Scott M, Torchia T, Prusiner SB (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

    PubMed  Google Scholar 

  20. Shinagawa M, Takahashi K, Sasaki S, Doi S, Goto H, Sato G (1985) Characterization of scrapie agent isolated from sheep in Japan. Microbiol Immunol 29: 543–551

    PubMed  Google Scholar 

  21. Stahl N, Baldwin MA, Teplow DB, Hood L, Gibson BW, Burlingame AL, Prusiner SB (1993) Structural studies of the scrapie prion protein using mass spectrometry and amino acid sequencing. Biochemistry 32: 1991–2002

    PubMed  Google Scholar 

  22. Tam JP (1988) Synthetic peptide vaccine design: Synthesis and properties of a high-density multiple antigenic peptide system. Proc Natl Acad Sci USA 85: 5409–5413

    PubMed  Google Scholar 

  23. Westaway D, Goodman PA, Mirenda CA, McKinley MP, Carlson GA, Prusiner SB (1987) Distinct prion proteins in short and long scrapie incubation period mice. Cell 51: 651–662

    PubMed  Google Scholar 

  24. Yokoyama T, Kimura K, Tagawa Y, Yuasa N (1995) Preparation and characterization of antibodies against mouse prion protein (PrP) peptides. Clin Diagn Lab Immunol 2: 172–176

    PubMed  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. National Institute of Animal Health, Ibaraki

    T. Yokoyama & N. Yuasa

  2. Institute for Virus Research, Kyoto University, Kyoto, Japan

    S. Itohara

Authors
  1. T. Yokoyama
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. S. Itohara
    View author publications

    You can also search for this author in PubMed Google Scholar

  3. N. Yuasa
    View author publications

    You can also search for this author in PubMed Google Scholar

Rights and permissions

Reprints and permissions

About this article

Cite this article

Yokoyama, T., Itohara, S. & Yuasa, N. Detection of species specific epitopes of mouse and hamster prion proteins (PrPs) by anti-peptide antibodies. Archives of Virology 141, 763–769 (1996). https://doi.org/10.1007/BF01718334

Download citation

  • Received:

  • Accepted:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF01718334

Keywords

Search

Navigation