The hemagglutinin-neuraminidase (HN) glycoprotein of Newcastle Disease Virus (NDV) is responsible for both the attachment and the sialidase activities of the virus, along with playing a multi-faceted role in the promotion of membrane fusion by the fusion protein (F). The sites responsible for these activities have not yet been identified in detail, although several regions important to those functions have been determined. Site-directed mutagenesis was used to introduce the mutation, I175E into the HN protein. As expected from comparison with the influenza NA protein, I175E-mutated HN is deficient in NA activity. However, it also lacks receptor binding and, consequently, fusion promoting activity. To test the possibility that the lack of receptor binding is due to steric hindrance of the attachment site resulting from failure to completely trim sialic acid from the protein's glycosyl groups, deletion of individual glycoprotein groups from the mutant was performed. Each of these failed to restore attachment, suggesting that I175 may play a role in attachment, as well as NA.

• 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

• Morgan, Jennifer Michelle
• Carlson, Gisela Maria

Publisher

• Worcester Polytechnic Institute

Identifier

• 99D017M

Advisor

• Adams, David S.

Year

• 1999

Sponsor

• University of Massachusetts Medical Center

Date created

• 1999-01-01

Resource type

• Major Qualifying Project

Major

• Biology & Biotechnology

Rights statement

• In Copyright