Estrada D Fernando, Boudreaux Daniel M, Zhong Dalian, St Jeor Stephen C, De Guzman Roberto N
Department of Molecular Biosciences, University of Kansas, Lawrence, Kansas 66045.
J Biol Chem. 2009 Mar 27;284(13):8654-60. doi: 10.1074/jbc.M808081200. Epub 2009 Jan 29.
Hantaviruses are distributed worldwide and can cause a hemorrhagic fever or a cardiopulmonary syndrome in humans. Mature virions consist of RNA genome, nucleocapsid protein, RNA polymerase, and two transmembrane glycoproteins, G1 and G2. The ectodomain of G1 is surface-exposed; however, it has a 142-residue C-terminal cytoplasmic tail that plays important roles in viral assembly and host-pathogen interaction. Here we show by NMR, circular dichroism spectroscopy, and mutagenesis that a highly conserved cysteine/histidine-rich region in the G1 tail of hantaviruses forms two CCHC-type classical zinc fingers. Unlike classical zinc fingers, however, the two G1 zinc fingers are intimately joined together, forming a compact domain with a unique fold. We discuss the implication of the hantaviral G1 zinc fingers in viral assembly and host-pathogen interaction.
汉坦病毒分布于全球，可导致人类出现出血热或心肺综合征。成熟的病毒粒子由RNA基因组、核衣壳蛋白、RNA聚合酶以及两种跨膜糖蛋白G1和G2组成。G1的胞外结构域暴露于表面；然而，它有一个142个残基的C端胞质尾巴，在病毒组装和宿主-病原体相互作用中发挥重要作用。在这里，我们通过核磁共振、圆二色光谱和诱变实验表明，汉坦病毒G1尾巴中一个高度保守的富含半胱氨酸/组氨酸的区域形成了两个CCHC型经典锌指结构。然而，与经典锌指不同的是，这两个G1锌指紧密相连，形成了一个具有独特折叠的紧凑结构域。我们讨论了汉坦病毒G1锌指在病毒组装和宿主-病原体相互作用中的意义。
