Complementary hydropathy identifies a cellular prion protein receptor
Author: ["Vilma R. Martins","Edgard Graner","José Garcia-Abreu","Sandro J. De Souza","Adriana F. Mercadante","Silvio S. Veiga","Silvio M. Zanata","Vivaldo Moura Neto","Ricardo R. Brentani"]
Publication: Nature Medicine
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Abstract
Prions, the etiological agents for infectious degenerative encephalopathies, act by entering the cell and inducing conformational changes in PrPc (a normal cell membrane sialoglycoprotein), which result in cell death. A specific cell-surface receptor to mediate PrPc and prion endocytosis has been predicted. Complementary hydropathy let us generate a hypothetical peptide mimicking the receptor binding site. Antibodies raised against this peptide stain the surface of mouse neurons and recognize a 66-kDa membrane protein that binds PrPc both in vitro and in vivo. Furthermore, both the complementary prion peptide and antiserum against it inhibit the toxicity of a prion-derived peptide toward neuronal cells in culture. Such reagents might therefore have therapeutic applications.
Cite this article
Martins, V., Graner, E., Garcia-Abreu, J. et al. Complementary hydropathy identifies a cellular prion protein receptor. Nat Med 3, 1376–1382 (1997). https://doi.org/10.1038/nm1297-1376
