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

被引:23
作者
Mirza, Anne M. [1 ]
Iorio, Ronald M. [1 ]
机构
[1] Univ Massachusetts, Sch Med, Dept Microbiol & Physiol Syst, Immunol & Microbiol Program, Worcester, MA 01605 USA
基金
美国国家卫生研究院;
关键词
HOMOLOGOUS FUSION PROTEIN; MONOCLONAL-ANTIBODIES; PARAMYXOVIRUS FUSION; RECEPTOR RECOGNITION; SENDAI-VIRUS; CELL-FUSION; GLYCOPROTEIN; DOMAIN; PROMOTION; FORM;
D O I
10.1128/JVI.01066-13
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
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.
引用
收藏
页码:8813 / 8815
页数:3
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