Award details

Chaperone interactions with PrP

Reference	BBS/E/I/00000652
Principal Investigator / Supervisor	Dr Christopher Birkett
Co-Investigators / Co-Supervisors
Institution	The Pirbright Institute
Department	The Pirbright Institute Department
Funding type	Research
Value (£)	33,622
Status	Completed
Type	Institute Project
Start date	01/06/1997
End date	31/05/2000
Duration	36 months

Abstract

The prion protein (PrP) plays a central role in TSE disease progression and transmission. It is now clear that conformational changes in the PrP molecule are pivotal in disease pathogenesis. Molecular chaperones have been shown to be important facilitators of protein conformational change in many cellular systems, but their effects upon PrP conformation are little studied. This proposal aims to test the hypothesis that chaperones can modulate PrP conformation and may be involved in disease related conformational changes by studying the biochemical basis of their interaction in vitro. We will analyse chaperone/PrP binding by a variety of methods and delineate the chaperone binding sites in PrP. The effects of hsp70 and co-chaperones on the re-folding of recombinant PrP after denaturation will also be investigated, including analysis of PrPsc and peptide mediated alterations in PrPc conformation. Studies of prion-like phenomena in yeast have suggested that manipulation of heat shock proteins and chaperones can inhibit prion activity. Therefore, demonstration that chaperones can mediate changes in PrP conformation may highlight new strategies to combat TSE.

Summary

unavailable

Committee	Closed Committee - Agri-food (AF)
Research Topics	X – not assigned to a current Research Topic
Research Priority	X – Research Priority information not available
Research Initiative	X - not in an Initiative
Funding Scheme	X – not Funded via a specific Funding Scheme

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