The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
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DOI：
10.1038/nsmb.1484
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发表时间：
2008-10-01
影响因子：
16.8
通讯作者：
Jones, Ian M.
中科院分区：
文献类型：
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作者：
Kadlec, Jan;Loureiro, Silvia;Jones, Ian M.
对于所有有包膜病毒，病毒融合蛋白在进入细胞期间介导宿主和病毒膜的合并。杆状病毒糖蛋白 gp64 (gp64) 在促进进入昆虫和哺乳动物细胞方面是不寻常的，并且与已建立的 I 类和 II 类融合蛋白不同。我们报告了其融合后形式的晶体结构，这解释了 gp64 的许多生物学特性，包括其细胞混杂性，鉴定了融合肽并表明它是新一类 (III) 融合蛋白的第三个代表，与水疱性口炎病毒 G 和单纯疱疹病毒 1 型 gB 蛋白具有意想不到的结构同源性。我们发现 III 类蛋白的结构域在 I 类和 II 类蛋白中都有对应的结构域，这表明所有这些病毒融合机器在结构上比以前认为的更相关。
Viral fusion proteins mediate the merger of host and viral membranes during cell entry for all enveloped viruses. Baculovirus glycoprotein gp64 (gp64) is unusual in promoting entry into both insect and mammalian cells and is distinct from established class I and class II fusion proteins. We report the crystal structure of its postfusion form, which explains a number of gp64's biological properties including its cellular promiscuity, identifies the fusion peptides and shows it to be the third representative of a new class (III) of fusion proteins with unexpected structural homology with vesicular stomatitis virus G and herpes simplex virus type 1 gB proteins. We show that domains of class III proteins have counterparts in both class I and II proteins, suggesting that all these viral fusion machines are structurally more related than previously thought.