Characterization of the molecular features of the pestivirus Erns protein with regard to ist function as structural component of the virion and virulence factor

瘟病毒 Erns 蛋白作为病毒粒子和毒力因子结构成分的功能的分子特征表征

• 批准号: 313902382
• 负责人: Professor Dr. Gregor Meyers
• 金额: --
• 依托单位: Friedrich-Loeffler-Institut - Bundesforschungsinstitut für Tiergesundheit (FLI)
• 依托单位国家: 德国
• 项目类别: Research Grants
• 财政年份: 2016
• 资助国家: 德国
• 起止时间: 2015-12-31 至 2017-12-31
• 项目状态: 已结题
• 来源: https://gepris.dfg.de/gepris/projekt/313902382?language=en
• 关键词: Characterization; molecular; features; pestivirus; Erns

The Erns protein of pestiviruses represents a specifically interesting viral protein since it combines the role of a structural surface protein with functions in repression of the type 1 interferon response, establishment of persistent infection and virulence in the natural host with the latter three features linked to the RNase activity of this protein. The mechanisms underlying both functions of the protein are not known in detail and will be investigated in the planned studies. Major questions in context with the function as a structural protein concern the role of Erns in virion assembly and budding and identification of the structure responsible for sorting of the protein into the virus particle. A special focus of the work will be on the importance of the unusual Erns membrane anchor with its conserved amino acid motifs for these processes. The virulence factor function of Erns is so far regarded to depend on its intrinsic RNase activity, its dimerization and its partial secretion form the host cell. The planned work aims at elucidation of the biochemical and cell biological basis of these features of Erns. The results of this work will contribute to understanding general aspects of pestivirus biology and the interaction of these viruses with the immune system of their hosts.

瘟病毒的 Erns 蛋白是一种特别有趣的病毒蛋白，因为它结合了结构表面蛋白的作用和抑制 1 型干扰素反应、在自然宿主中建立持续感染和毒力的功能，后三个特征与该蛋白的 RNase 活性相关。该蛋白质两种功能的机制尚不清楚，将在计划的研究中进行研究。与作为结构蛋白的功能有关的主要问题涉及 Erns 在病毒体组装和出芽中的作用以及负责将蛋白质分选到病毒颗粒中的结构的识别。这项工作的一个特别重点是不寻常的 Erns 膜锚及其保守氨基酸基序对这些过程的重要性。迄今为止，Erns 的毒力因子功能被认为取决于其内在的 RNase 活性、其二聚化及其从宿主细胞的部分分泌。计划的工作旨在阐明 Erns 这些特征的生化和细胞生物学基础。这项工作的结果将有助于了解瘟病毒生物学的一般方面以及这些病毒与其宿主免疫系统的相互作用。

项目成果

Restoration of glycoprotein Erns dimerization via pseudoreversion partially restores virulence of classical swine fever virus.

通过假回复恢复糖蛋白 Erns 二聚化可部分恢复猪瘟病毒的毒力

• DOI: 10.1099/jgv.0.000990
• 发表时间: 2018
• 期刊: The Journal of general virology
• 作者: Tucakov AK;Yavuz S;Schürmann EM;Mischler M;Klingebeil A;Meyers G
• 通讯作者: Meyers G

Downstream Sequences Control the Processing of the Pestivirus Erns-E1 Precursor

• DOI: 10.1128/jvi.01905-20
• 发表时间: 2020-10
• 期刊: Journal of Virology
• 影响因子: 5.4
• 作者: Yu Mu;Ioana Bintintan;G. Meyers

Type I and III IFNs Produced by Plasmacytoid Dendritic Cells in Response to a Member of the Flaviviridae Suppress Cellular Immune Responses

• DOI: 10.4049/jimmunol.1600049
• 发表时间: 2016-05
• 期刊: The Journal of Immunology
• 作者: E. Reid;N. Juleff;M. Windsor;S. Gubbins;L. Roberts;S. Morgan;G. Meyers;E. Pérez-Martín;E. Tchi