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
UMass Chan Affiliations
Department of Microbiology and Physiological SystemsDocument Type
Journal ArticlePublication Date
2013-08-01Keywords
Amino Acid SubstitutionHN Protein
Mutant Proteins
Newcastle disease virus
Protein Binding
*Protein Multimerization
Viral Fusion Proteins
*Virus Internalization
Virology
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Show full item recordAbstract
Newcastle 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.Source
Mirza 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 siteDOI
10.1128/JVI.01066-13Permanent Link to this Item
http://hdl.handle.net/20.500.14038/30145PubMed ID
23740987Related Resources
Link to Article in PubMedRights
Publisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.Scopus Count
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