Interaction of decay-accelerating factor with coxsackievirus B3
Interaction of decay-accelerating factor with coxsackievirus B3
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DOI：
10.1128/jvi.00931-07
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发表时间：
2007-12-01
影响因子：
5.4
通讯作者：
Rossmann, Michael G.
中科院分区：
文献类型：
--
作者：
Hafenstein, Susan;Bowman, Valorie D.;Rossmann, Michael G.
许多肠道病毒、副埃科病毒和鼻病毒使用免疫球蛋白（IG）样受体结合到病毒峡谷中，并在感染期间启动病毒脱壳。然而，这些病毒中的一些使用替代或额外的受体，结合在峡谷之外。柯萨奇病毒-腺病毒受体（CAR），一种结合到病毒峡谷中的Ig样分子，和衰变加速因子（decay-accelerating factor，ERF）已被鉴定为柯萨奇病毒B3（CVB 3）的细胞受体。与DAF复合的CVB 3变体的冷冻电子显微镜重建显示，60个结合位点中的每个位点都完全占据DAF受体。DAY分子桥接峡谷，阻断CAR结合位点，导致两种受体相互竞争。CVB 3上的结合位点与埃可病毒表面上的结合位点不同，表明独立的进化过程。
Many entero-, parecho-, and rhinoviruses use inummoglobulin (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 DAY 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.