GSBS Student Publications
Title
Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
UMMS Affiliation
Graduate School of Biomedical Sciences; Department of Molecular Genetics and Microbiology
Date
11-16-2004
Document Type
Article
Medical Subject Headings
Amino Acid Sequence; Amino Acid Substitution; Animals; Cricetinae; HN Protein; *Membrane Fusion; Molecular Sequence Data; Neuraminidase; Newcastle disease virus; Receptors, Virus; Viral Fusion Proteins
Disciplines
Life Sciences | Medicine and Health Sciences
Abstract
The hemagglutinin-neuraminidase (HN) protein of Newcastle disease virus mediates attachment to sialic acid receptors, as well as cleavage of the same moiety. HN also interacts with the other viral glycoprotein, the fusion (F) protein, to promote membrane fusion. The ectodomain of the HN spike consists of a stalk and a terminal globular head. The most conserved part of the stalk consists of two heptad repeats separated by a nonhelical intervening region (residues 89 to 95). Several amino acid substitutions for a completely conserved proline residue in this region not only impair fusion and the HN-F interaction but also decrease neuraminidase activity in the globular domain, suggesting that the substitutions may alter HN structure. Substitutions for L94 also interfere with fusion and the HN-F interaction but have no significant effect on any other HN function. Amino acid substitutions at other positions in the intervening region also modulate only fusion. In all cases, diminished fusion correlates with a decreased ability of the mutated HN protein to interact with F at the cell surface. These findings indicate that the intervening region is critical to the role of HN in the promotion of fusion and may be directly involved in its interaction with the homologous F protein.
Rights and Permissions
Citation: J Virol. 2004 Dec;78(23):13053-61. Link to article on publisher's site
DOI of Published Version
10.1128/JVI.78.23.13053-13061.2004
Related Resources
Journal Title
Journal of virology
PubMed ID
15542657
Repository Citation
Melanson, Vanessa Rose and Iorio, Ronald M., "Amino acid substitutions in the F-specific domain in the stalk of the newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein" (2004). GSBS Student Publications. 846.
https://escholarship.umassmed.edu/gsbs_sp/846