期刊
JOURNAL OF VIROLOGY
卷 87, 期 15, 页码 8813-8815出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JVI.01066-13
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资金
- National Institutes of Health [AI-49268]
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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