Faculty Advisor

Adams, David S.

Abstract

Newcastle Disease (NDV) is a member of the Paramyxovirus genome of the family Paramyxoviridae. Mumps virus and the various human and animal parainfluenza viruses are other Paramyxoviruses. These viruses exhibit three distinctive properties: hemagglutination, the cleavage of sialic acid, and fusion. The hemagglutinin-neuraminidase (HN) and the fusion (F) proteins are responsible for these three activities. The ectodomain of the HN spike can be separated into a terminal globular domain and a membrane-proximal stalk-like structure. The x-ray crystallographic structure of the globular domain has recently been solved. Substitutions for the NA active site residues result in a loss of both NA and HAd. In the crystallographic structure, this suggests that the NA and attachment sites are the same, only in different conformation. Findings from this analysis indicate that mutations at the interface between the monomers of the HN abolish fusion. They also severely diminish HAd at 37?C. The mutants do exhibit HAd at 4?C, suggesting that the substitutions induce the protein to assume the NA conformation.

Publisher

Worcester Polytechnic Institute

Date Accepted

January 2002

Major

Biotechnology

Project Type

Major Qualifying Project

Accessibility

Restricted-WPI community only

Advisor Department

Biology and Biotechnology

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