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The 208–222 Region of the Peplomer Glycoprotein as a Putative Binding Site of Rabies Virus with the Nicotinic Acetylcholine Receptor

  • P. Neri
  • L. Bracci
  • A. Di Tommaso
  • L. Lozzi
  • M. Rustici
  • A. Santucci
  • P. Soldani
  • S. Petreni
  • N. Niccolai
  • P. Mascagni
  • G. Siligardi
  • W. A. Gibbons
Chapter
Part of the Experimental Biology and Medicine book series (EBAM, volume 19)

Abstract

There is increasing evidence that viruses utilize recep tors for physiological ligands in order to infect their host cells. For instance, it has been shown that vaccinia virus binds to the receptors of epidermal growth factor (1), Eppstein-Barr virus to the receptor for the complement on B-lymphocytes (2), and those of HTLV-III and rabies to the T4 antigen of T lymphocytes (3) and acetylcholine receptor (4), respectively. Since the acetyl choline receptor is the target organ of many other non-physiological ligands as, for instance, the neurotoxins of snake venoms, the structure of which is well-known, we decided to compare the amino acid sequence of the glycoprotein peplomers of rabies virus (RGV) with that of snake neurotoxins (NTX) in order to detect homologies, which in turn can lead to the identification of the binding site of the viral protein with the receptor.

Keywords

Circular Dichro Spectrum Nicotinic Acetylcholine Receptor Rabies Virus Peptide Binding Site Cationic Moiety 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. 1.
    Eppstein, D.A., Marsh, Y.V., Schreiber, A.B., Newman, S.R., Todaro, G.J. and Nestor, J.J. Jr. (1985) Nature 318, 663–665.PubMedCrossRefGoogle Scholar
  2. 2.
    Fingeroth, J.D. et al. (1984) Proc. Natl. Acad. Sci. USA 81, 4510–4514.PubMedCrossRefGoogle Scholar
  3. 3.
    Klatzmann, et al.(1984) Nature 312, 767–768.PubMedCrossRefGoogle Scholar
  4. 4.
    Lentz, T.L., Burrage, T.G., Smith, A.L., Crick, J. and Tignor, G.H. (1982) Science 215, 182–184.PubMedCrossRefGoogle Scholar
  5. 5.
    Malcolm, D., Walkinshaw, W.S. and Maelicke, A. (1980) Proc. Natl. Acad. Sci. USA 77, 2400–2404.CrossRefGoogle Scholar
  6. 6.
    Tsernoglou, D., Petsko, G.A. and Hudson, R.A. (1978) Mol. Pharm. 14, 710.Google Scholar
  7. 7.
    Hopp, T.P. and Woods, K.R. (1981) Proc. Natl. Acad. Sci. USA 78, 3824–3828.PubMedCrossRefGoogle Scholar
  8. 8.
    Chou, P.Y. and Fasman, G.D. (1978) Adv. Enzymol. 47, 48–148.Google Scholar
  9. 9.
    Avrameas, S. and Ternynck, T. (1969) Immunochemistry 6, 53.PubMedCrossRefGoogle Scholar
  10. 10.
    Cianfriglia, M., Mariani, M. Armellini, D., Masson, E.A., Lafata, M., Presentini, R. and Antoni, G. (1986) Meth. Enzym. 121, 193.PubMedCrossRefGoogle Scholar
  11. 11.
    Han, K.K., Richard, C. and Delacourte, A. (1984) Int. J. Biochem. 2, 129.CrossRefGoogle Scholar
  12. 12.
    Lindstrom, J., Einarson, B. and Tzartos, S. (1981) Meth. Enzymol. (1981) 74, 432–460.PubMedCrossRefGoogle Scholar
  13. 13.
    Kabat, E.A., Wu, T.T. and Bilofsky, H. (1976) in: Variable Regions of Immunoglobulin Chains, Bolt Beranck and Newman, Cambridge, MA.Google Scholar
  14. 14.
    Rose, J.K., Doolittle, R.F., Anilionis, A., Curtis, P.J. and Wunner, W.H. (1982) J. of Virology 43, 361–364.Google Scholar
  15. 15.
    Woody, R.W. (1974) in: Peptides, Polypeptides and Proteins, Wiley, New York, pp. 338–358.Google Scholar
  16. 16.
    Gierasch, C.M., Debev, C.M., Madison, V., Niv, C.H. and Blout, E.R. (1981) Biochemistry 20, 4730–4738PubMedCrossRefGoogle Scholar
  17. 17.
    Roderick, I. and MacFarlan, et al. (1984) J. Immunol. 133, 2748–2752.Google Scholar
  18. 18.
    Kieber Emmons, T. and Kohle, R.H. (1986) Proc. Natl. Acad. Sci. USA 83, 2521–2525.CrossRefGoogle Scholar

Copyright information

© The Humana Press Inc. 1987

Authors and Affiliations

  • P. Neri
    • 1
    • 2
  • L. Bracci
    • 3
  • A. Di Tommaso
    • 1
  • L. Lozzi
    • 1
  • M. Rustici
    • 1
  • A. Santucci
    • 1
  • P. Soldani
    • 3
  • S. Petreni
    • 1
  • N. Niccolai
    • 2
  • P. Mascagni
    • 4
  • G. Siligardi
    • 4
  • W. A. Gibbons
    • 4
  1. 1.CRISMAUniversità di SienaItaly
  2. 2.Dipartimento di ChimicaUniversità di SienaItaly
  3. 3.Dipartimento Biologia EvolutivaUniversità di SienaItaly
  4. 4.School of PharmacyUniversity of LondonUK

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