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Protein glycosylation in Leishmania spp.
Molecular Omics ( IF 3.0 ) Pub Date : 2020-07-24 , DOI: 10.1039/d0mo00043d
Simon Ngao Mule 1 , Joyce Silva Saad 1 , Livia Rosa Fernandes 1 , Beatriz S Stolf 2 , Mauro Cortez 2 , Giuseppe Palmisano 1
Affiliation  

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.

中文翻译:

利什曼原虫中的蛋白质糖基化。

蛋白质糖基化是翻译后修饰,在利什曼原虫的寄生虫中,在载体-寄生虫-脊椎动物宿主相互作用中起关键作用。在哺乳动物宿主中,利什曼原虫蛋白糖基化参与毒力,宿主细胞入侵以及免疫逃逸和调节。在利什曼原虫糖萼由糖缀合物的密集阵列包括lipophosphoglycan,glycoinositolphospholipids,糖蛋白和其在组合物之间变化proteophosphoglycans由利什曼原虫属物种和发育阶段。关于利什曼原虫蛋白糖基化的当前知识是非常有限的。开发新型分析工具以表征利什曼原虫糖蛋白组学和调节寄生虫糖代码的扩展工具箱将有助于破译利什曼原虫-宿主相互作用的过程。这篇综述将概述利什曼原虫蛋白质糖基化和所报道的聚糖结构的当前知识,以及基于质谱的分析在整个利什曼原虫糖蛋白组和糖组分析中的潜在应用。
更新日期:2020-07-24
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