糖基化
生物
聚糖
基因
病毒
病毒学
遗传学
计算生物学
细胞生物学
糖蛋白
作者
Lucas T. Jae,Matthijs Raaben,Moniek Riemersma,Ellen van Beusekom,Vincent A. Blomen,Arno Velds,Ron Kerkhoven,Jan E. Carette,Haluk Topaloǧlu,Peter Meinecke,Marja W. Wessels,Dirk Lefeber,Sean P. J. Whelan,Hans van Bokhoven,Thijn R. Brummelkamp
出处
期刊:Science
[American Association for the Advancement of Science (AAAS)]
日期:2013-04-26
卷期号:340 (6131): 479-483
被引量:260
标识
DOI:10.1126/science.1233675
摘要
Glycosylated α-dystroglycan (α-DG) serves as cellular entry receptor for multiple pathogens, and defects in its glycosylation cause hereditary Walker-Warburg syndrome (WWS). At least eight proteins are critical to glycosylate α-DG, but many genes mutated in WWS remain unknown. To identify modifiers of α-DG, we performed a haploid screen for Lassa virus entry, a hemorrhagic fever virus causing thousands of deaths annually that hijacks glycosylated α-DG to enter cells. In complementary screens, we profiled cells for absence of α-DG carbohydrate chains or biochemically related glycans. This revealed virus host factors and a suite of glycosylation units, including all known Walker-Warburg genes and five additional factors critical for the modification of α-DG. Our findings accentuate the complexity of this posttranslational feature and point out genes defective in dystroglycanopathies.
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