Department of Microbiology and Physiological Systems
Amino Acid Substitution; HN Protein; Mutant Proteins; Newcastle disease virus; Protein Binding; *Protein Multimerization; Viral Fusion Proteins; *Virus Internalization
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.
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DOI of Published Version
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
Journal of virology
Mirza AM, Iorio RM. (2013). 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. University of Massachusetts Medical School Faculty Publications. https://doi.org/10.1128/JVI.01066-13. Retrieved from https://escholarship.umassmed.edu/faculty_pubs/385