戊型肝炎病毒大结构域载脂蛋白和adp核糖结合形式的1H, 13C, 15N骨干共振分配

IF 0.8 4区 生物学 Q4 BIOPHYSICS Biomolecular NMR Assignments Pub Date : 2022-10-22 DOI:10.1007/s12104-022-10111-5
Maria D. Politi, Angelo Gallo, Georgios Bouras, Maria Birkou, Bruno Canard, Bruno Coutard, Georgios A. Spyroulias
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引用次数: 0

摘要

戊型肝炎病毒(HEV)的基因组长7.2千碱基,有三个开放阅读框。最大的一个是ORF1,它编码一种参与复制过程的非结构蛋白,其加工过程不明确。ORF1蛋白是一种包含宏结构域(MD)的多模块蛋白。MDs是所有生物王国中进化上保守的结构。MDs参与adp核糖基化的识别和去除,特别是病毒MDs被鉴定为adp核糖片段的擦除者,这解释了它们在逃避宿主免疫反应的早期阶段是重要的参与者。对天然HEV MD的载脂蛋白和adp核糖结合状态的详细结构分析将提供结构信息,以了解HEV MD如何参与病毒-宿主相互作用以及在病毒复制过程中它如何与细胞内伙伴相互作用。本文报道了HEV原生宏结构域的高产表达及其溶液核磁共振光谱分析。HEV MD在溶液中折叠,我们给出了载脂蛋白和结合态的几乎完整的主链和侧链分配。此外,利用TALOS +分析进行了二级结构预测。结果表明,HEV MD具有与大多数病毒宏结构域非常相似的α/β/α拓扑结构。
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1H, 13C, 15N backbone resonance assignment of apo and ADP-ribose bound forms of the macro domain of Hepatitis E virus through solution NMR spectroscopy

The genome of Hepatitis E virus (HEV) is 7.2 kilobases long and has three open reading frames. The largest one is ORF1, encoding a non-structural protein involved in the replication process, and whose processing is ill-defined. The ORF1 protein is a multi-modular protein which includes a macro domain (MD). MDs are evolutionarily conserved structures throughout all kingdoms of life. MDs participate in the recognition and removal of ADP-ribosylation, and specifically viral MDs have been identified as erasers of ADP-ribose moieties interpreting them as important players at escaping the early stages of host-immune response. A detailed structural analysis of the apo and bound to ADP-ribose state of the native HEV MD would provide the structural information to understand how HEV MD is implicated in virus-host interplay and how it interacts with its intracellular partner during viral replication. In the present study we present the high yield expression of the native macro domain of HEV and its analysis by solution NMR spectroscopy. The HEV MD is folded in solution and we present a nearly complete backbone and sidechains assignment for apo and bound states. In addition, a secondary structure prediction by TALOS + analysis was performed. The results indicated that HEV MD has a α/β/α topology very similar to that of most viral macro domains.

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来源期刊
Biomolecular NMR Assignments
Biomolecular NMR Assignments 生物-光谱学
CiteScore
1.70
自引率
11.10%
发文量
59
审稿时长
6-12 weeks
期刊介绍: Biomolecular NMR Assignments provides a forum for publishing sequence-specific resonance assignments for proteins and nucleic acids as Assignment Notes. Chemical shifts for NMR-active nuclei in macromolecules contain detailed information on molecular conformation and properties. Publication of resonance assignments in Biomolecular NMR Assignments ensures that these data are deposited into a public database at BioMagResBank (BMRB; http://www.bmrb.wisc.edu/), where they are available to other researchers. Coverage includes proteins and nucleic acids; Assignment Notes are processed for rapid online publication and are published in biannual online editions in June and December.
期刊最新文献
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