Correlation of structural elements and infectivity of the HET-s prion

Christiane Ritter, Marie-Lise Maddelein, Ansgar B. Siemer, Thorsten Lührs, Matthias Ernst, Beat H. Meier, Sven J. Saupe and Roland Riek ()
Additional contact information
Christiane Ritter: The Salk Institute
Marie-Lise Maddelein: Centre national de la Recherche Scientifique Université de Bordeaux 2
Ansgar B. Siemer: ETH Zurich, Physical Chemistry, ETH Honggerberg
Thorsten Lührs: The Salk Institute
Matthias Ernst: ETH Zurich, Physical Chemistry, ETH Honggerberg
Beat H. Meier: ETH Zurich, Physical Chemistry, ETH Honggerberg
Sven J. Saupe: Centre national de la Recherche Scientifique Université de Bordeaux 2
Roland Riek: The Salk Institute

Nature, 2005, vol. 435, issue 7043, 844-848

Abstract: Probing prions Alzheimer's, prion diseases and other neurodegenerative disorders are associated with insoluble protein fibres called amyloid fibrils. Gathering structural information about these has proved difficult, but three groups now report success with contrasting approaches to the problem. The cover shows the atomic structure of the ‘spine’ of an amyloid-like fibril formed by the yeast prion protein Sup35. To obtain this structure, Nelson et al. performed X-ray crystallography on amyloid microcrystals. Krishnan and Lindquist used a raft of techniques to study folding of the amyloid core. And Ritter et al. determined the infectious conformation of HET-s prion of a filamentous fungus. Christopher Dobson ponders on what this flood of structural data says about prion and amyloid formation in sickness and in health.

Date: 2005
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DOI: 10.1038/nature03793

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