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首页> 外文期刊>Biochemistry >Identification of the glycosylation site of the adenovirus type 5 fiber protein
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Identification of the glycosylation site of the adenovirus type 5 fiber protein

机译：鉴定5型腺病毒纤维蛋白的糖基化位点

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摘要

The fiber protein purified from the pool of nonincorporated viral protein after infection of cells with adenovirus type 5 exists as two forms separable by reverse-phase HPLC. As determined by mass spectrometry, this heterogeneity results from a difference in one O-linked N-acetylglucosamine (GlcNac). A western blot analysis using a monoclonal antibody directed against the GlcNac motif showed that only one of the two forms reacted with the antibody, suggesting that one form carries a single GlcNac and the other form has none. The ratio of glycosylated to nonglycosylated forms of fiber, which is about 1, is conserved in assembled viruses. After digestion of glycosylated fiber with endoproteinase GluC, isolation of the glycosylated peptide by reverse-phase HPLC, and chemical derivatization using dimethylamine, the site of glycosylation was located in the fiber shaft at serine 109 by mass spectrometry. Elimination of glycosylation by site-directed mutagenesis of fiber should help to understand the function of this postranslational modification.
机译：在用5型腺病毒感染细胞后，从未掺入病毒的蛋白质池中纯化的纤维蛋白以两种形式存在，可通过反相HPLC分离。如通过质谱法所确定的，这种异质性是由于一种O-连接的N-乙酰氨基葡糖胺（GlcNac）的差异造成的。使用针对GlcNac基序的单克隆抗体进行的蛋白质印迹分析表明，两种形式中只有一种与抗体反应，表明一种形式携带单个GlcNac，而另一种形式则没有。在组装的病毒中，纤维的糖基化形式与非糖基化形式之比约为1。用内蛋白酶GluC消化糖基化的纤维，通过反相HPLC分离糖基化的肽，并使用二甲胺进行化学衍生化后，通过质谱法将糖基化的位点定位在丝氨酸109的纤维轴中。通过纤维的定点诱变消除糖基化应有助于理解这种翻译后修饰的功能。

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