Glycosylation of viral surface proteins probed by mass spectrometry
Glycosylation of viral surface proteins probed by mass spectrometry
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DOI：
10.1016/j.coviro.2019.05.003
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发表时间：
2019-06-01
影响因子：
5.9
通讯作者：
Renfrow, Matthew B.
中科院分区：
文献类型：
--
作者：
Hargett, Audra A.;Renfrow, Matthew B.
糖基化是在许多病毒表面蛋白（VSP）上发现的常见且具有生物学意义的翻译后修饰。这些聚糖中的许多通过调节病毒受体结合、掩蔽抗原位点或通过刺激宿主免疫应答来影响毒力。质谱（MS）已成为表征VSP糖基化的关键技术。这篇综述将涵盖如何基于MS的分析，如释放的聚糖概况，聚糖位点定位，位点占用率和位点特异性异质性，被用来映射VSP糖基化。此外，这篇评论将提供有关如何MS糖分析数据正在与分子和结构实验结合使用，以提供更好地了解特定的聚糖在VSP功能中的作用的信息。
Glycosylation is a common and biologically significant post translational modification that is found on numerous virus surface proteins (VSPs). Many of these glycans affect virulence through modulating virus receptor binding, masking antigenic sites, or by stimulating the host immune response. Mass spectrometry (MS) has arisen as a pivotal technique for the characterization of VSP glycosylation. This review will cover how MS-based analyses, such as released glycan profiles, glycan site localization, site-occupancy, and site-specific heterogeneity, are being utilized to map VSP glycosylation. Furthermore, this review will provide information on how MS glycoprofiling data are being used in conjunction with molecular and structural experiments to provide a better understanding of the role of specific glycans in VSP function.