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Protein Science (2004), 13:1933-1938. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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FOR THE RECORD

Observation of sequence specificity in the seeding of protein amyloid fibrils

Mark R.H. Krebs1, Ludmilla A. Morozova-Roche2, Katie Daniel, Carol V. Robinson3 and Christopher M. Dobson3

Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, Oxford OX1 3QH, United Kingdom

(RECEIVED February 27, 2004; FINAL REVISION April 8, 2004; ACCEPTED April 8, 2004)



Abstract

It is well established that the rate of formation of fibrils by amyloidogenic proteins is enhanced by the addition of preformed fibrils, a phenomenon known as seeding. We show that the efficiency of seeding fibril formation from solutions of hen lysozyme by a series of other proteins depends strongly on the similarity of their sequences. This observation is consistent with the importance of long-range interactions in stabilizing the core structure of amyloid fibrils and may be associated with the existence of a species barrier observed in the transmissible spongiform encephalopathies. In addition, it is consistent with the observation of a single dominant type of protein in the deposits associated with each form of amyloid disease.

Keywords: amyloid; lysozyme; seeding; cross-seeding; species barrier

Reprint requests to: Christopher M. Dobson, Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB2 1EW, UK; e-mail: cmd44{at}cam.ac.uk; fax: 44 (0) 1223-763418.

1 Present addresses: P and C Group, Cavendish Laboratory, University of Cambridge, Cambridge CB3 0HE, UK;

2 Department of Medical Biochemistry and Biophysics, Umeå University, Umeå SE 90187, Sweden;

3 Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK.

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04707004.


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