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多食棘阿米巴拟病毒中的O-连接糖基化

O-Linked glycosylation in Acanthamoeba polyphaga mimivirus.

作者信息

Hülsmeier Andreas J, Hennet Thierry

机构信息

Institute of Physiology, University of Zurich, Winterthurerstrasse 190, Zurich 8057, Switzerland

Institute of Physiology, University of Zurich, Winterthurerstrasse 190, Zurich 8057, Switzerland.

出版信息

Glycobiology. 2014 Aug;24(8):703-14. doi: 10.1093/glycob/cwu034. Epub 2014 May 2.

Abstract

Acanthamoeba polyphaga mimivirus is a member of the giant nucleocytoplasmic large DNA viruses, infecting various Acanthamoeba spp. The genomes of giant viruses encode components previously thought to be exclusive to cellular life, such as proteins involved in nucleic acid and protein synthesis. Recent work on enzymes involved in carbohydrate biosynthesis and metabolism show that instead of utilizing host cell resources, Mimivirus produces its own glycosylation machinery. To obtain a more detailed view of glycosylation in Mimivirus, we developed a periodate oxidation-based method to selectively enrich Mimivirus surface glycoproteins. O-Glycosylation in Mimivirus glycoproteins was identified by permethylation and matrix-assisted laser desorption/ionization-mass spectrometry analyses of beta-eliminated glycans. We sequenced 26 previously undescribed O-glycans, most of which contain glucose as their reducing end saccharide. These data will facilitate future studies on the functional significance of glycosylation in Mimivirus.

摘要

多食棘阿米巴拟菌病毒是巨型核质大DNA病毒的成员之一,可感染多种棘阿米巴属物种。巨型病毒的基因组编码了一些以前被认为是细胞生命所特有的成分,比如参与核酸和蛋白质合成的蛋白质。最近关于参与碳水化合物生物合成和代谢的酶的研究表明,拟菌病毒并非利用宿主细胞资源,而是产生了自己的糖基化机制。为了更详细地了解拟菌病毒中的糖基化情况,我们开发了一种基于高碘酸盐氧化的方法来选择性富集拟菌病毒表面糖蛋白。通过对β-消除聚糖的全甲基化和基质辅助激光解吸/电离质谱分析,鉴定了拟菌病毒糖蛋白中的O-糖基化。我们对26种以前未描述的O-聚糖进行了测序,其中大多数以葡萄糖作为其还原端糖类。这些数据将有助于未来对拟菌病毒中糖基化功能意义的研究。

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