Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.

Science 28 July 2000:
Vol. 289. no. 5479, pp. 556 - 557
DOI: 10.1126/science.289.5479.556
Prev | Table of Contents | Next

Perspectives

Also see the archival list of Science's Compass: Enhanced Perspectives

CELL BIOLOGY:
Enhanced: Sowing the Protein Seeds of Prion Propagation

Mick F. Tuite

Ever since Prusiner first proposed his radical "protein-only" hypothesis to explain how certain infectious proteins (prions) are transmitted from one mammal to another in the absence of DNA or RNA, scientists have been trying to prove him right (or wrong). The study of mammalian prions, such as those causing Creutzfeldt-Jakob disease in humans, scrapie in sheep and mad cow disease in cattle, has been slow to yield answers. However, as Tuite discusses in his Perspective, the Sup35p and Ure2p proteins of yeast that exist in both normal and infectious forms are providing evidence that the "protein-only" hypothesis may be right (Sparrer et al.).

The author is at the Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK. E-mail: m.f.tuite{at}ukc.ac.uk

Read the Full Text


THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
The elongation of yeast prion fibers involves separable steps of association and conversion.
T. Scheibel, J. Bloom, and S. L. Lindquist (2004)
PNAS 101, 2287-2292
   Abstract »    Full Text »    PDF »
Amyloid aggregates of the HET-s prion protein are infectious.
M.-L. Maddelein, S. Dos Reis, S. Duvezin-Caubet, B. Coulary-Salin, and S. J. Saupe (2002)
PNAS 99, 7402-7407
   Abstract »    Full Text »    PDF »


To Advertise     Find Products

Science. ISSN 0036-8075 (print), 1095-9203 (online)