新城疫病毒血凝素神经氨酸酶（HN）蛋白茎部的突变阻止了 F 蛋白的触发，尽管它允许高效的 HN-F 复合物形成。
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.
机构信息
Department of Microbiology and Physiological Systems, Immunology and Microbiology Program, University of Massachusetts Medical School, Worcester, Massachusetts, USA.
出版信息
J Virol. 2013 Aug;87(15):8813-5. doi: 10.1128/JVI.01066-13. Epub 2013 Jun 5.
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.
摘要
新城疫病毒（NDV）诱导的膜融合需要血凝素神经氨酸酶（HN）和融合（F）蛋白之间形成复合物。NDV HN 茎部残基 A89、L90 和 L94 的取代通过调节 HN-F 复合物的形成来阻止融合。在这里，我们证明了附近的 L97A 取代虽然先前被证明可以阻止融合，但允许有效的 HN-F 复合物形成，并且可能通过防止触发结合 F 蛋白所需的 HN 茎部的变化来发挥作用。
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