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Temporal role played by specific structural proteins during assembly of African swine fever virus

Reference	BBS/E/I/00000056
Principal Investigator / Supervisor	Professor Tom Wileman
Co-Investigators / Co-Supervisors
Institution	The Pirbright Institute
Department	The Pirbright Institute Department
Funding type	Research
Value (£)	66,982
Status	Completed
Type	Institute Project
Start date	01/10/1997
End date	30/09/2000
Duration	36 months

Abstract

The capsids of icosahedral viruses provide excellent examples of the complexity of protein folding and assembly in cells. The simplest capsids contain 60 identical subunits, while the largest contain many thousands. In order to be assembled into virions individual capsid subunts must be folded correctly. It is generally believed that host chaperones are required during the initial folding of capsid proteins as they emerge from ribosomes. Indeed, the essential role of molecular chaperones for the assembly of viral capsids was revealed more than 20 years ago when mutations in E. coli which prevented lytic infection with bacteriophage lambda identified the bacterial chaperones DnaK, DnaJ and GroEL. African Swine Fever (ASF) virus is one of the largest and most complex icosahedral viruses and provides an excellent system to study the role played by chaperones during virus assembly.

Summary

unavailable

Committee	Closed Committee - Animal Sciences (AS)
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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