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Role of the matrix protein in morbillivirus morphogenesis and stability
Reference
BBS/E/I/00000734
Principal Investigator / Supervisor
Professor Thomas Barrett
Co-Investigators /
Co-Supervisors
Institution
The Pirbright Institute
Department
The Pirbright Institute Department
Funding type
Research
Value (£)
106,430
Status
Completed
Type
Institute Project
Start date
01/10/1999
End date
30/09/2002
Duration
36 months
Abstract
Rinderpest (RP) and peste des petits ruminants (PPR) viruses are the causes of serious diseases of major economic importance in cattle and small ruminants, respectively. In order to study genetic factors which determine host range, reverse genetics technology has been used to generate chimeric RP virus containing the two surface glycoproteins of PPR. This virus is severely debilitated, compared to either of the parent viruses, both in cell culture and in goat vaccination experiments. The matrix protein is thought to bring the internal virus nucleocapsids into contact with the virus envelope glycoproteins and the non-homology of this protein for the PPR glycoproteins may be responsible for the defects in the virus. The present project aims to swap the RP matrix protein with that of the PPR virus in the existing chimera and test the fitness of the resulting virus. In addition, since there are two distinct domains in the matrix protein, chimeric RP/PPR matrix protein genes will be produced and substituted for the RP matrix protein in other chimeras. In this way it is hoped to identify which domain is responsible for interaction with the internal nucleocapsids and which domain with the surface glycoproteins.
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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