The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers
The Hantavirus Glycoprotein G1 Tail Contains Dual CCHC-type Classical Zinc Fingers
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DOI：
10.1074/jbc.m808081200
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发表时间：
2009-03-27
影响因子：
4.8
通讯作者：
De Guzman, Roberto N.
中科院分区：
文献类型：
--
作者：
Estrada, D. Fernando;Boudreaux, Daniel M.;De Guzman, Roberto N.
汉坦病毒分布在世界各地，可引起人类出血热或心肺综合征。成熟病毒粒子由RNA基因组、核衣壳蛋白、RNA聚合酶和两种跨膜糖蛋白G1和G2组成。G1的外畴是表面暴露的；然而，它具有142个残基的c端细胞质尾部，在病毒组装和宿主-病原体相互作用中起重要作用。通过核磁共振、圆二色光谱和诱变，我们发现汉坦病毒G1尾部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。然而，与传统的锌指不同，两个G1锌指紧密地连接在一起，形成一个具有独特褶皱的紧凑结构域。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。
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.