Structural insights into calicivirus attachment and uncoating
Structural insights into calicivirus attachment and uncoating
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DOI：
10.1128/jvi.00550-08
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发表时间：
2008-08-01
影响因子：
5.4
通讯作者：
Goodfellow, Ian G.
中科院分区：
文献类型：
--
作者：
Bhella, David;Gatherer, Derek;Goodfellow, Ian G.
杯状病毒科包括具有医学和兽医学意义的正义RNA病毒。在人类中，杯状病毒是急性胃肠炎的主要原因，而在动物中，呼吸道疾病、结膜炎、口腔炎和出血性疾病也有记载。病毒-宿主相互作用的研究受到该家族中许多病毒缺乏培养系统的限制。猫杯状病毒（FCV）是Vesivirus属的成员，提供了一个易于处理的模型，因为它可以在细胞培养物中繁殖。猫连接粘附分子1（fJAM-1）是近年来发现的FCV的功能性受体。我们分析了这种病毒受体复合物的结构，冷冻电子显微镜和三维图像重建，结合拟合的同源建模的高分辨率坐标。我们表明，fJAM-1的结构域1结合到FCV衣壳蛋白VP 1的P2结构域的外表面，诱导病毒衣壳中的构象变化。这项研究提供了第一个天然杯状病毒-蛋白受体复合物的结构视图，并深入了解病毒附着和脱壳的机制。
The Caliciviridae family comprises positive-sense RNA viruses of medical and veterinary significance. In humans, caliciviruses are a major cause of acute gastroenteritis, while in animals respiratory illness, conjunctivitis, stomatitis, and hemorrhagic disease are documented. Investigation of virus-host interactions is limited by a lack of culture systems for many viruses in this family. Feline calicivirus (FCV), a member of the Vesivirus genus, provides a tractable model, since it may be propagated in cell culture. Feline junctional adhesion molecule 1 (fJAM-1) was recently identified as a functional receptor for FCV. We have analyzed the structure of this virus-receptor complex by cryo-electron microscopy and three-dimensional image reconstruction, combined with fitting of homology modeled high-resolution coordinates. We show that domain 1 of fJAM-1 binds to the outer face of the P2 domain of the FCV capsid protein VP1, inducing conformational changes in the viral capsid. This study provides the first structural view of a native calicivirus-protein receptor complex and insights into the mechanisms of virus attachment and uncoating.