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Probing the mechanism of the paramyxovirus haemagglutinin-neuraminidase
Reference
B13850
Principal Investigator / Supervisor
Professor Garry Taylor
Co-Investigators /
Co-Supervisors
Institution
University of St Andrews
Department
Biology
Funding type
Research
Value (£)
198,932
Status
Completed
Type
Research Grant
Start date
01/10/2000
End date
28/02/2004
Duration
41 months
Abstract
Paramyxoviruses are the leading cause of respiratory disease of children. One of the two viral surface glycoproteins, the haemagglutinin-neuraminidase (HN), has several functions key to infection. We have recently determined the first crystal structure of a prototypic HN, that serves as a model for HN from human parainfluenza viruses. Our studies suggest that HN has a single sialic acid recognition site, that through conformational changes can switch between a binding site and a catalytic site. Our studies also suggest that a change in the HN dimer association could be the trigger for fusion promotion. We propose to probe these functions by site-directed mutagenesis.
Summary
unavailable
Committee
Closed Committee - Biomolecular Sciences (BMS)
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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