title: 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.
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.
authors.affiliation: Department of Microbiology and Physiological Systems, Immunology and Microbiology Program, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
authors.forename: Anne M
authors.initials: AM
authors.lastname: Mirza
authors.forename: Ronald M
authors.initials: RM
authors.lastname: Iorio
mesh_terms: D019943:Amino Acid Substitution; D015707:HN Protein / Q000235:genetics / Q000378:metabolism*; D050505:Mutant Proteins / Q000235:genetics / Q000378:metabolism; D009522:Newcastle disease virus / Q000235:genetics / Q000502:physiology*; D011485:Protein Binding; D055503:Protein Multimerization; D014760:Viral Fusion Proteins / Q000378:metabolism*; D053586:Virus Internalization
chemical_list: D015707:HN Protein; D050505:Mutant Proteins; D014760:Viral Fusion Proteins