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 37C. The mutants do exhibit HAd at 4C, suggesting that the substitutions induce the protein to assume the NA conformation.

• This report represents the work of one or more WPI undergraduate students submitted to the faculty as evidence of completion of a degree requirement. WPI routinely publishes these reports on its website without editorial or peer review.

Creator

• Levandowsky, Elizabeth C.

Publisher

• Worcester Polytechnic Institute

Identifier

• 02D260M

Advisor

• Adams, David S.

Year

• 2002

Sponsor

• University of Massachusetts Medical Center

Date created

• 2002-01-01

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright