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首页> 外文期刊>Journal of Molecular Biology >Structural characterization of the glycoprotein GP2 core domain from the CAS virus, a novel arenavirus-like species.
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Structural characterization of the glycoprotein GP2 core domain from the CAS virus, a novel arenavirus-like species.

机译：来自CAS病毒的糖蛋白GP2核心结构域的结构表征，CAS病毒是一种新型的空域病毒样物种。

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Fusion of the viral and host cell membranes is a necessary first step for infection by enveloped viruses and is mediated by the envelope glycoprotein. The transmembrane subunits from the structurally defined "class I" glycoproteins adopt an α-helical "trimer-of-hairpins" conformation during the fusion pathway. Here, we present our studies on the envelope glycoprotein transmembrane subunit, GP2, of the CAS virus (CASV). CASV was recently identified from annulated tree boas (Corallus annulatus) with inclusion body disease and is implicated in the disease etiology. We have generated and characterized two protein constructs consisting of the predicted CASV GP2 core domain. The crystal structure of the CASV GP2 post-fusion conformation indicates a trimeric α-helical bundle that is highly similar to those of Ebola virus and Marburg virus GP2 despite CASV genome homology to arenaviruses. Denaturation studies demonstrate that the stability of CASV GP2 is pH dependent with higher stability at lower pH; we propose that this behavior is due to a network of interactions among acidic residues that would destabilize the α-helical bundle under conditions where the side chains are deprotonated. The pH-dependent stability of the post-fusion structure has been observed in Ebola virus and Marburg virus GP2, as well as other viruses that enter via the endosome. Infection experiments with CASV and the related Golden Gate virus support a mechanism of entry that requires endosomal acidification. Our results suggest that, despite being primarily arenavirus like, the transmembrane subunit of CASV is extremely similar to the filoviruses.
机译：病毒和宿主细胞膜的融合是包膜病毒感染的必要第一步，并由包膜糖蛋白介导。来自结构上定义的“ I类”糖蛋白的跨膜亚单位在融合途径中采用α-螺旋“发夹三聚体”构象。在这里，我们介绍我们对CAS病毒（CASV）的包膜糖蛋白跨膜亚基GP2的研究。最近从带有包涵体疾病的无环乔木（Corallus annulatus）中鉴定出CASV，并与疾病病因有关。我们已经生成并表征了由预测的CASV GP2核心结构域组成的两个蛋白质构建体。尽管CASV基因组与沙粒病毒同源，但CASV GP2融合后构象的晶体结构表明三聚体α螺旋束与埃博拉病毒和马尔堡病毒GP2高度相似。变性研究表明，CASV GP2的稳定性取决于pH值，在较低pH值下具有较高的稳定性。我们认为，这种行为是由于酸性残基之间的相互作用网络造成的，该酸性残基在侧链去质子化的条件下会破坏α-螺旋束的稳定性。在埃博拉病毒和马尔堡病毒GP2以及通过内体进入的其他病毒中，已经观察到融合后结构的pH依赖性稳定性。 CASV和相关金门病毒的感染实验支持需要内体酸化的进入机制。我们的结果表明，尽管主要是类鼻病毒，但CASV的跨膜亚单位与丝状病毒极为相似。

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