GlycoProteomics Laboratory, Department of Parasitology, Institute of Biomedical Sciences, University of Sao Paulo, Avenida Lineu Prestes 1374, Butantã, Sao Paulo - 05508-000, Brazil.
Department of Parasitology, Institute of Biomedical Sciences, University of Sao Paulo, Sao Paulo, Brazil.
Mol Omics. 2020 Oct 12;16(5):407-424. doi: 10.1039/d0mo00043d.
Protein glycosylation is a co- and post-translational modification that, in Leishmania parasites, plays key roles in vector-parasite-vertebrate host interaction. In the mammalian host, Leishmania protein glycosylation is involved in virulence, host cell invasion, and immune evasion and modulation. The Leishmania glycocalyx is composed by a dense array of glycoconjugates including lipophosphoglycan, glycoinositolphospholipids, glycoproteins and proteophosphoglycans which varies in composition between Leishmania species and developmental stages. The current knowledge on Leishmania protein glycosylation is quite limited. The development of novel analytical tools to characterize the Leishmania glycoproteome and the expanding toolbox to modulate the parasite glycocode will help in deciphering the processes involved in Leishmania-host interaction. This review will recapitulate the current knowledge of Leishmania protein glycosylation, and glycan structures reported, and the potential application of mass spectrometry-based analysis for system-wide Leishmania glycoproteome and glycome analysis.
蛋白质糖基化是一种共翻译和翻译后修饰，在利什曼原虫寄生虫中，在媒介-寄生虫-脊椎动物宿主相互作用中起着关键作用。在哺乳动物宿主中，利什曼原虫的蛋白质糖基化参与了毒力、宿主细胞入侵以及免疫逃避和调节。利什曼原虫糖萼由包括脂磷壁酸、糖基肌醇磷脂、糖蛋白和蛋白磷酸聚糖在内的大量糖缀合物组成，其组成在利什曼原虫物种和发育阶段之间有所不同。目前对利什曼原虫蛋白质糖基化的了解相当有限。开发新型分析工具来描述利什曼原虫糖蛋白组，以及扩展调节寄生虫糖码的工具包，将有助于破译利什曼原虫-宿主相互作用中涉及的过程。本文综述了利什曼原虫蛋白质糖基化及其报道的聚糖结构的最新知识，以及基于质谱的分析在利什曼原虫糖蛋白组和糖组系统分析中的潜在应用。
