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蛋白质组学方法解析先天抗病毒免疫反应中宿主 SUMOylation 。

Proteomic Approaches to Dissect Host SUMOylation during Innate Antiviral Immune Responses.

机构信息

Institute of Medical Virology, University of Zürich, 8057 Zürich, Switzerland.

出版信息

Viruses. 2021 Mar 23;13(3):528. doi: 10.3390/v13030528.

DOI:10.3390/v13030528
PMID:33806893
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC8004987/
Abstract

SUMOylation is a highly dynamic ubiquitin-like post-translational modification that is essential for cells to respond to and resolve various genotoxic and proteotoxic stresses. Virus infections also constitute a considerable stress scenario for cells, and recent research has started to uncover the diverse roles of SUMOylation in regulating virus replication, not least by impacting antiviral defenses. Here, we review some of the key findings of this virus-host interplay, and discuss the increasingly important contribution that large-scale, unbiased, proteomic methodologies are making to discoveries in this field. We highlight the latest proteomic technologies that have been specifically developed to understand SUMOylation dynamics in response to cellular stresses, and comment on how these techniques might be best applied to dissect the biology of SUMOylation during innate immunity. Furthermore, we showcase a selection of studies that have already used SUMO proteomics to reveal novel aspects of host innate defense against viruses, such as functional cross-talk between SUMO proteins and other ubiquitin-like modifiers, viral antagonism of SUMO-modified antiviral restriction factors, and an infection-triggered SUMO-switch that releases endogenous retroelement RNAs to stimulate antiviral interferon responses. Future research in this area has the potential to provide new and diverse mechanistic insights into host immune defenses.

摘要

SUMOylation 是一种高度动态的泛素样翻译后修饰,对于细胞应对和解决各种遗传毒性和蛋白毒性应激至关重要。病毒感染也是细胞面临的一个相当大的应激情况,最近的研究开始揭示 SUMOylation 在调节病毒复制中的多种作用,尤其是通过影响抗病毒防御。在这里,我们回顾了这一病毒-宿主相互作用的一些关键发现,并讨论了大规模、无偏倚的蛋白质组学方法在该领域的发现中所做出的越来越重要的贡献。我们强调了一些专门用于了解细胞应激反应中 SUMOylation 动态的最新蛋白质组学技术,并评论了这些技术如何最好地应用于剖析固有免疫过程中 SUMOylation 的生物学。此外,我们展示了一些已经使用 SUMO 蛋白质组学来揭示宿主先天防御病毒的新方面的研究,例如 SUMO 蛋白和其他泛素样修饰物之间的功能交叉对话、病毒拮抗 SUMO 修饰的抗病毒限制因子,以及感染触发的 SUMO 开关,释放内源性逆转录元件 RNA 以刺激抗病毒干扰素反应。该领域的未来研究有可能为宿主免疫防御提供新的和多样化的机制见解。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/3c3732e83ddb/viruses-13-00528-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/cd4874aebef3/viruses-13-00528-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/2de3e4f40f6b/viruses-13-00528-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/bc9bae6db8b5/viruses-13-00528-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/25d455b40d21/viruses-13-00528-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/81984d64581c/viruses-13-00528-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/3c3732e83ddb/viruses-13-00528-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/cd4874aebef3/viruses-13-00528-g001.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/2de3e4f40f6b/viruses-13-00528-g002.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/bc9bae6db8b5/viruses-13-00528-g003.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/25d455b40d21/viruses-13-00528-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/81984d64581c/viruses-13-00528-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/a607/8004987/3c3732e83ddb/viruses-13-00528-g006.jpg

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本文引用的文献

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Identification of proximal SUMO-dependent interactors using SUMO-ID.使用 SUMO-ID 鉴定近端 SUMO 依赖性相互作用蛋白。
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