N-Glycoproteomics of Human Seminal Plasma Glycoproteins
N-Glycoproteomics of Human Seminal Plasma Glycoproteins
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DOI：
10.1021/acs.jproteome.5b01069
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发表时间：
2016-03-01
影响因子：
4.4
通讯作者：
Renkonen, Risto
中科院分区：
文献类型：
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作者：
Saraswat, Mayank;Joenvaara, Sakari;Renkonen, Risto
精浆通过抑制过早获能来帮助精子，帮助脑内运输和输卵管精子库的形成，所有这些似乎在受精过程中都很重要。已知诸如刘易斯x和y的表位存在于精浆糖蛋白上，其可以调节母体免疫应答。多项研究表明，精浆糖蛋白在受精过程中发挥着重要作用，但这一作用在很大程度上尚未被发现。我们已经设计了一种策略来分析糖肽从一个复杂的，未知的混合物的蛋白酶消化的蛋白质。该分析提供了对糖蛋白、糖基化位点、聚糖组成和来自原始样品的拟定结构的鉴定。这种策略已被应用于人精浆总糖蛋白。我们已经阐明了聚糖组成和建议的结构，243糖肽属于73 N糖基化位点的50糖蛋白。大多数拟定聚糖结构为复合型（83%），其次为高甘露糖型（10%），然后为杂合型（7%）。大多数糖蛋白是唾液酸化的、岩藻糖基化的或两者都有。发现许多带有聚糖的刘易斯x/ a和y/B表位，表明多种精浆糖蛋白上的免疫调节表位。该研究还表明，大规模的N-糖基化映射是可实现的与当前的技术和分析的深度大致成比例的预分馏和样品的复杂性。
Seminal plasma aids sperm by inhibiting premature capacitation, helping in the intracervical transport and formation of an oviductal sperm reservoir, all of which appear to be important in the fertilization process. Epitopes such as Lewis x and y are known to be present on seminal plasma glycoproteins, which can modulate the maternal immune response. It is suggested by multiple studies that seminal plasma glycoproteins play, largely undiscovered, important roles in the process of fertilization. We have devised a strategy to analyze glycopeptides from a complex, unknown mixture of protease-digested proteins. This analysis provides identification of the glycoproteins, glycosylation sites, glycan compositions, and proposed structures from the original sample. This strategy has been applied to human seminal plasma total glycoproteins. We have elucidated glycan compositions and proposed structures for 243 glycopeptides belonging to 73 Nglycosylation sites on 50 glycoproteins. The majority of the proposed glycan structures were complex type (83%) followed by high-mannose (10%) and then hybrid (7%). Most of the glycoproteins were either sialylated, fucosylated, or both. Many Lewis x/ a and y/b epitopes bearing glycans were found, suggesting immune-modulating epitopes on multiple seminal plasma glycoproteins. The study also shows that large scale N-glycosylation mapping is achievable with current techniques and the depth of the analysis is roughly proportional to the prefractionation and complexity of the sample.