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    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

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    J._Virol._2013_Mirza_8813_5.pdf
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    Authors
    Mirza, Anne M.
    Iorio, Ronald M.
    UMass Chan Affiliations
    Department of Microbiology and Physiological Systems
    Document Type
    Journal Article
    Publication Date
    2013-08-01
    Keywords
    Amino Acid Substitution
    HN Protein
    Mutant Proteins
    Newcastle disease virus
    Protein Binding
    *Protein Multimerization
    Viral Fusion Proteins
    *Virus Internalization
    Virology
    
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    Abstract
    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 site
    DOI
    10.1128/JVI.01066-13
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/30145
    PubMed ID
    23740987
    Related Resources
    Link to Article in PubMed
    Rights
    Publisher PDF posted as allowed by the publisher's author rights policy at http://journals.asm.org/site/misc/ASM_Author_Statement.xhtml.
    ae974a485f413a2113503eed53cd6c53
    10.1128/JVI.01066-13
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