Intramolecular versus intermolecular disulfide bonds in prion proteins

Ervin Welker, Lynne D. Raymond, Harold A. Scheraga, Byron Caughey

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75 Citations (Scopus)


Prion protein (PrP) is the major component of the partially protease-resistant aggregate that accumulates in mammals with transmissible spongiform encephalopathies. The two cysteines of the scrapie form, PrPSc, were found to be in their oxidized (i.e. disulfide) form (Turk, E., Teplow, D. B., Hood, L. E., and Prusiner, S. B. (1988) Eur. J. Biochem. 176, 21-30); however, uncertainty remains as to whether the disulfide bonds are intra- or intermolecular. It is demonstrated here that the monomers of PrPSc are not linked by intermolecular disulfide bonds. Furthermore, evidence is provided that PrPSc can induce the conversion of the oxidized, disulfide-intact form of the monomeric cellular prion protein to its protease-resistant form without the temporary breakage and subsequent re-formation of the disulfide bonds in cell-free reactions.

Original languageEnglish
Pages (from-to)33477-33481
Number of pages5
JournalJournal of Biological Chemistry
Issue number36
Publication statusPublished - Sep 6 2002


ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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