EBV gB的特性表明其兼具I类和II类病毒融合蛋白的性质。
Characterization of EBV gB indicates properties of both class I and class II viral fusion proteins.
作者信息
Backovic Marija, Leser George P, Lamb Robert A, Longnecker Richard, Jardetzky Theodore S
机构信息
Department of Biochemistry, Molecular Biology, Cell Biology, Northwestern University, Evanston, IL 60208, USA.
出版信息
Virology. 2007 Nov 10;368(1):102-13. doi: 10.1016/j.virol.2007.06.031. Epub 2007 Jul 25.
To gain insight into Epstein-Barr virus (EBV) glycoprotein B (gB), recombinant, secreted variants were generated. The role of putative transmembrane regions, the proteolytic processing and the oligomerization state of the gB variants were investigated. Constructs containing 2 of 3 C-terminal hydrophobic regions were secreted, indicating that these do not act as transmembrane anchors. The efficiency of cleavage of the gB furin site was found to depend on the nature of C-terminus. All of the gB constructs formed rosette structures reminiscent of the postfusion aggregates formed by other viral fusion proteins. However, substitution of putative fusion loop residues, WY(112-113) and WLIY(193-196), with less hydrophobic amino acids from HSV-1 gB, produced trimeric protein and abrogated the ability of the EBV gB ectodomains to form rosettes. These data demonstrate biochemical features of EBV gB that are characteristic of other class I and class II viral fusion proteins, but not of HSV-1 gB.
为深入了解爱泼斯坦-巴尔病毒（EBV）糖蛋白B（gB），我们构建了重组分泌变体。对gB变体中假定的跨膜区域的作用、蛋白水解加工过程以及寡聚化状态进行了研究。包含3个C端疏水区域中2个的构建体能够分泌，这表明这些区域并非作为跨膜锚定结构。研究发现，gB弗林蛋白酶切割位点的切割效率取决于C端的性质。所有gB构建体均形成玫瑰花结结构，这让人联想到其他病毒融合蛋白形成的融合后聚集体。然而，用来自单纯疱疹病毒1型（HSV-1）gB的疏水性较低的氨基酸取代假定的融合环残基WY（112-113）和WLIY（193-196）后，产生了三聚体蛋白，并消除了EBV gB胞外域形成玫瑰花结的能力。这些数据表明，EBV gB具有其他I类和II类病毒融合蛋白的生化特征，但不具有HSV-1 gB的生化特征。
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