Structural and biophysical characterization of the Borna disease virus 1 phosphoprotein

IF 1.1 4区 生物学 Q4 BIOCHEMICAL RESEARCH METHODS
Jack D. Whitehead, Jonathan M. Grimes, Jeremy R. Keown
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Abstract

Bornaviruses are RNA viruses with a mammalian, reptilian, and avian host range. The viruses infect neuronal cells and in rare cases cause a lethal encephalitis. The family Bornaviridae are part of the Mononegavirales order of viruses, which contain a nonsegmented viral genome. Mononegavirales encode a viral phosphoprotein (P) that binds both the viral polymerase (L) and the viral nucleoprotein (N). The P protein acts as a molecular chaperone and is required for the formation of a functional replication/transcription complex. In this study, the structure of the oligomerization domain of the phosphoprotein determined by X-ray crystallography is reported. The structural results are complemented with biophysical characterization using circular dichroism, differential scanning calorimetry and small-angle X-ray scattering. The data reveal the phosphoprotein to assemble into a stable tetramer, with the regions outside the oligomerization domain remaining highly flexible. A helix-breaking motif is observed between the α-helices at the midpoint of the oligomerization domain that appears to be conserved across the Bornaviridae. These data provide information on an important component of the bornavirus replication complex.

Abstract Image

博尔纳病病毒1型磷蛋白的结构和生物物理特性
Bornavirus是哺乳动物、爬行动物和鸟类宿主的RNA病毒。这种病毒会感染神经元细胞,在极少数情况下会导致致命的脑炎。Bornaviridae家族是病毒单体目的一部分,该目包含一个未分段的病毒基因组。单阴性病毒编码一种结合病毒聚合酶(L)和病毒核蛋白(N)的病毒磷蛋白(P)。P蛋白作为分子伴侣,是形成功能性复制/转录复合物所必需的。在本研究中,报道了通过X射线晶体学测定的磷蛋白低聚结构域的结构。使用圆二色性、差示扫描量热法和小角度X射线散射对结构结果进行了生物物理表征。数据显示磷蛋白组装成稳定的四聚体,低聚结构域外的区域保持高度柔性。在寡聚结构域中点的α-螺旋之间观察到一个螺旋断裂基序,该基序在Bornaviridae中似乎是保守的。这些数据提供了关于冠状病毒复制复合体的一个重要组成部分的信息。
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来源期刊
Acta crystallographica. Section F, Structural biology communications
Acta crystallographica. Section F, Structural biology communications BIOCHEMICAL RESEARCH METHODSBIOCHEMISTRY &-BIOCHEMISTRY & MOLECULAR BIOLOGY
CiteScore
1.90
自引率
0.00%
发文量
95
期刊介绍: Acta Crystallographica Section F is a rapid structural biology communications journal. Articles on any aspect of structural biology, including structures determined using high-throughput methods or from iterative studies such as those used in the pharmaceutical industry, are welcomed by the journal. The journal offers the option of open access, and all communications benefit from unlimited free use of colour illustrations and no page charges. Authors are encouraged to submit multimedia content for publication with their articles. Acta Cryst. F has a dedicated online tool called publBio that is designed to make the preparation and submission of articles easier for authors.
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