Key Laboratory of Zoonosis Research, Ministry of Education, Central Laboratory, Jilin University Second Hospital, Jilin University, Changchun 130062, PR China.
Clinical Medical College, Jilin University, Changchun 130021, PR China.
J Proteome Res. 2021 Jan 1;20(1):110-121. doi: 10.1021/acs.jproteome.0c00778. Epub 2020 Dec 21.
Influenza viruses continue evolving and have the ability to cause a global pandemic, so it is very important to elucidate its pathogenesis and find new treatment methods. In recent years, proteomics has made important contributions to describing the dynamic interaction between influenza viruses and their hosts, especially in posttranslational regulation of a variety of key biological processes. Protein posttranslational modifications (PTMs) increase the diversity of functionality of the organismal proteome and affect almost all aspects of pathogen biology, primarily by regulating the structure, function, and localization of the modified proteins. Considerable technical achievements in mass spectrometry-based proteomics have been made in a large number of proteome-wide surveys of PTMs in many different organisms. Herein we specifically focus on the proteomic studies regarding a variety of PTMs that occur in both the influenza viruses, mainly influenza A viruses (IAVs), and their hosts, including phosphorylation, ubiquitination and ubiquitin-like modification, glycosylation, methylation, acetylation, and some types of acylation. Integration of these data sets provides a unique scenery of the global regulation and interplay of different PTMs during the interaction between IAVs and their hosts. Various techniques used to globally profiling these PTMs, mostly MS-based approaches, are discussed regarding their increasing roles in mechanical regulation of interaction between influenza viruses and their hosts.
流感病毒在不断进化，有能力引发全球大流行，因此阐明其发病机制并寻找新的治疗方法非常重要。近年来，蛋白质组学在描述流感病毒与其宿主之间的动态相互作用方面做出了重要贡献，特别是在后翻译水平上调节多种关键生物过程的调控。蛋白质翻译后修饰（PTMs）增加了生物机体蛋白质组的功能多样性，并影响病原体生物学的几乎所有方面，主要通过调节修饰蛋白的结构、功能和定位。基于质谱的蛋白质组学在对许多不同生物体的蛋白质组范围内的 PTM 进行大量研究方面取得了相当大的技术成就。在这里，我们特别关注与流感病毒（主要是甲型流感病毒（IAV））及其宿主中发生的多种 PTM 相关的蛋白质组学研究，包括磷酸化、泛素化和泛素样修饰、糖基化、甲基化、乙酰化和一些类型的酰化。这些数据集的整合提供了 IAV 与其宿主相互作用过程中不同 PTM 全局调控和相互作用的独特景象。讨论了用于全局分析这些 PTM 的各种技术，主要是基于 MS 的方法，以及它们在机械调控流感病毒与其宿主相互作用方面的作用不断增加。
