新城疫病毒血凝素神经氨酸酶中的第二个唾液酸结合位点：对融合的影响。
Second sialic acid binding site in Newcastle disease virus hemagglutinin-neuraminidase: implications for fusion.
作者信息
Zaitsev Viatcheslav, von Itzstein Mark, Groves Darrin, Kiefel Milton, Takimoto Toru, Portner Allen, Taylor Garry
机构信息
Centre for Biomolecular Sciences, University of St. Andrews, St. Andrews, Fife KY16 9ST, United Kingdom.
出版信息
J Virol. 2004 Apr;78(7):3733-41. doi: 10.1128/jvi.78.7.3733-3741.2004.
Abstract
Paramyxoviruses are the leading cause of respiratory disease in children. Several paramyxoviruses possess a surface glycoprotein, the hemagglutinin-neuraminidase (HN), that is involved in attachment to sialic acid receptors, promotion of fusion, and removal of sialic acid from infected cells and progeny virions. Previously we showed that Newcastle disease virus (NDV) HN contained a pliable sialic acid recognition site that could take two states, a binding state and a catalytic state. Here we present evidence for a second sialic acid binding site at the dimer interface of HN and present a model for its involvement in cell fusion. Three different crystal forms of NDV HN now reveal identical tetrameric arrangements of HN monomers, perhaps indicative of the tetramer association found on the viral surface.
摘要
副粘病毒是儿童呼吸道疾病的主要病因。几种副粘病毒拥有一种表面糖蛋白，即血凝素神经氨酸酶（HN），它参与与唾液酸受体的结合、促进融合以及从受感染细胞和子代病毒粒子中去除唾液酸。此前我们表明，新城疫病毒（NDV）的HN含有一个柔韧的唾液酸识别位点，该位点可以呈现两种状态，即结合状态和催化状态。在此我们提供证据证明在HN的二聚体界面存在第二个唾液酸结合位点，并提出了其参与细胞融合的模型。新城疫病毒HN的三种不同晶体形式现在揭示了HN单体相同的四聚体排列，这可能表明在病毒表面发现的四聚体缔合。
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