A mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation
AuthorsMirza, Anne M.
Iorio, Ronald M.
UMass Chan AffiliationsDepartment of Microbiology and Physiological Systems
Document TypeJournal Article
KeywordsAmino Acid Substitution
Newcastle disease virus
Viral Fusion Proteins
MetadataShow full item record
AbstractNewcastle disease virus (NDV)-induced membrane fusion requires formation of a complex between the hemagglutinin-neuraminidase (HN) and fusion (F) proteins. Substitutions for NDV HN stalk residues A89, L90, and L94 block fusion by modulating formation of the HN-F complex. Here, we demonstrate that a nearby L97A substitution, though previously shown to block fusion, allows efficient HN-F complex formation and likely acts by preventing changes in the HN stalk required for triggering of the bound F protein.
SourceMirza AM, Iorio RM. A mutation in the stalk of the newcastle disease virus hemagglutinin-neuraminidase (HN) protein prevents triggering of the F protein despite allowing efficient HN-F complex formation. J Virol. 2013 Aug;87(15):8813-5. doi: 10.1128/JVI.01066-13. Link to article on publisher's site
Permanent Link to this Itemhttp://hdl.handle.net/20.500.14038/30145
Related ResourcesLink to Article in PubMed
RightsPublisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.
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