Hafenstein Susan, Bowman Valorie D, Chipman Paul R, Bator Kelly Carol M, Lin Feng, Medof M Edward, Rossmann Michael G
Department of Biological Sciences, Purdue University, 915 W. State Street, West Lafayette, IN 47907-2054, USA.
J Virol. 2007 Dec;81(23):12927-35. doi: 10.1128/JVI.00931-07. Epub 2007 Sep 5.
Many entero-, parecho-, and rhinoviruses use immunoglobulin (Ig)-like receptors that bind into the viral canyon and are required to initiate viral uncoating during infection. However, some of these viruses use an alternative or additional receptor that binds outside the canyon. Both the coxsackievirus-adenovirus receptor (CAR), an Ig-like molecule that binds into the viral canyon, and decay-accelerating factor (DAF) have been identified as cellular receptors for coxsackievirus B3 (CVB3). A cryoelectron microscopy reconstruction of a variant of CVB3 complexed with DAF shows full occupancy of the DAF receptor in each of 60 binding sites. The DAF molecule bridges the canyon, blocking the CAR binding site and causing the two receptors to compete with one another. The binding site of DAF on CVB3 differs from the binding site of DAF on the surface of echoviruses, suggesting independent evolutionary processes.
许多肠道病毒、副回声病毒和鼻病毒利用免疫球蛋白（Ig）样受体，这些受体结合到病毒峡谷中，在感染期间启动病毒脱壳是必需的。然而，其中一些病毒使用替代受体或额外受体，这些受体结合在峡谷之外。柯萨奇病毒腺病毒受体（CAR）是一种结合到病毒峡谷中的Ig样分子，衰变加速因子（DAF）已被确定为柯萨奇病毒B3（CVB3）的细胞受体。与DAF复合的CVB3变体的冷冻电子显微镜重建显示，在60个结合位点中的每一个位点上，DAF受体都被完全占据。DAF分子横跨峡谷，阻断CAR结合位点，导致两种受体相互竞争。CVB3上DAF的结合位点与回声病毒表面DAF的结合位点不同，这表明存在独立的进化过程。
