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A more recent version of this article appeared on August 6, 2004
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M403730200v1
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Papers In Press, published online ahead of print May 20, 2004
J. Biol. Chem, 10.1074/jbc.M403730200
Submitted on April 5, 2004
Revised on May 14, 2004
Accepted on May 20, 2004

Discriminating scrapie and BSE isolates by infrared spectroscopy of pathological prion protein

Achim Thomzig, Sashko Spassov, Manuela Friedrich, Dieter Naumann, and Michael Beekes

P26, Robert Koch-Institut, Berlin 13353

Corresponding Author: BeekesM{at}rki.de, beekesm@o2online.de

For the surveillance of transmissible spongiform encephalopathies (TSEs) in animals and humans the discrimination of different TSE strains causing scrapie, BSE or Creutzfeldt-Jakob disease constitutes a substantial challenge. We addressed this problem by Fourier-transform infrared (FT-IR) spectroscopy of pathological prion protein PrP27-30. Different isolates of hamster-adapted scrapie (263K, 22A-H, ME7-H) and BSE (BSE-H) were passaged in Syrian hamsters. Two of these agents, 22A-H and ME7-H, caused TSEs with indistinguishable clinical symptoms, neuropathological changes, and electrophoretic mobilities and glycosylation patterns of PrP27-30. However, FT-IR spectroscopy revealed that PrP27-30 of all four isolates featured different characteristics in the secondary structure, allowing a clear distinction between the passaged TSE agents. FT-IR analysis showed that phenotypic information is mirrored in beta-sheet and other secondary structure elements of PrP27-30, also in cases where immuno-biochemical typing failed to detect structural differences. If the findings of this study hold true for non-experimental TSEs in animals and humans, FT-IR characterisation of PrP27-30 may provide a versatile tool for molecular strain typing without antibodies and without restrictions to specific TSEs or mammalian species.


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