详情页 - 四川省肿瘤医院知识库

当前位置：首页 > 详情页

The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation.

文献详情

资源类型：

Pubmed体系：

收录情况： ◇ 自然指数

作者：

机构： [1]Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of L€ubeck, L€ubeck, Germany [2]German Center for Infection Research (DZIF), Hamburg–L€ubeck– Borstel–Riems Site, University of L€ubeck, L€ubeck, Germany [3]State Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University, Chengdu, China [4]Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich, Munich, Germany [5]German Center for Infection Research (DZIF), Munich, Germany [6]Gene Center Munich, Department of Biochemistry, Ludwig-Maximilians-University Munich, Munich, Germany [7]Institute of Veterinary Bacteriology, Vetsuisse Faculty, University of Bern, Bern, Switzerland [8]Institute of Virology and Immunology, University of Bern, Bern, Switzerland [9]Department of Biology and Center for Integrated Protein Science, Ludwig-Maximilians-University Munich, Planegg-Martinsried, Germany [10]College of Veterinary Medicine, Northwest A&F University, Yangling, Shaanxi, China [11]Institute of Molecular Medicine, University of L€ubeck, L€ubeck, Germany

出处：

DOI：

ISSN：

关键词： coronavirus eukaryotic translation initiation factors macrodomain protein synthesis virus-host interactions

摘要：

The ongoing outbreak of severe acute respiratory syndrome (SARS) coronavirus 2 (SARS-CoV-2) demonstrates the continuous threat of emerging coronaviruses (CoVs) to public health. SARS-CoV-2 and SARS-CoV share an otherwise non-conserved part of non-structural protein 3 (Nsp3), therefore named as "SARS-unique domain" (SUD). We previously found a yeast-2-hybrid screen interaction of the SARS-CoV SUD with human poly(A)-binding protein (PABP)-interacting protein 1 (Paip1), a stimulator of protein translation. Here, we validate SARS-CoV SUD:Paip1 interaction by size-exclusion chromatography, split-yellow fluorescent protein, and co-immunoprecipitation assays, and confirm such interaction also between the corresponding domain of SARS-CoV-2 and Paip1. The three-dimensional structure of the N-terminal domain of SARS-CoV SUD ("macrodomain II", Mac2) in complex with the middle domain of Paip1, determined by X-ray crystallography and small-angle X-ray scattering, provides insights into the structural determinants of the complex formation. In cellulo, SUD enhances synthesis of viral but not host proteins via binding to Paip1 in pBAC-SARS-CoV replicon-transfected cells. We propose a possible mechanism for stimulation of viral translation by the SUD of SARS-CoV and SARS-CoV-2. © 2021 The Authors. Published under the terms of the CC BY 4.0 license.

基金：

语种：

PubmedID：

中科院(CAS)分区：

出版当年[2021]版：

大类 | 1 区

生物学

小类 | 1 区生化与分子生物学 1 区细胞生物学

最新[2023]版：

大类 | 1 区

生物学

小类 | 1 区生化与分子生物学 1 区细胞生物学

第一作者：

第一作者机构： [1]Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of L€ubeck, L€ubeck, Germany [2]German Center for Infection Research (DZIF), Hamburg–L€ubeck– Borstel–Riems Site, University of L€ubeck, L€ubeck, Germany [3]State Key Laboratory of Biotherapy and Cancer Center, National Clinical Research Center for Geriatrics, West China Hospital, Sichuan University, Chengdu, China

共同第一作者：

通讯作者：

通讯机构： [1]Institute of Biochemistry, Center for Structural and Cell Biology in Medicine, University of L€ubeck, L€ubeck, Germany [2]German Center for Infection Research (DZIF), Hamburg–L€ubeck– Borstel–Riems Site, University of L€ubeck, L€ubeck, Germany [4]Max-von-Pettenkofer Institute, Ludwig-Maximilians-University Munich, Munich, Germany [5]German Center for Infection Research (DZIF), Munich, Germany [11]Institute of Molecular Medicine, University of L€ubeck, L€ubeck, Germany

推荐引用方式(GB/T 7714)：

APA：

MLA：

The SARS-unique domain (SUD) of SARS-CoV and SARS-CoV-2 interacts with human Paip1 to enhance viral RNA translation.

文献详情

相关文献