Glycans mediate a wide variety of biological roles via recognition by glycan-binding proteins (GBPs). Comprehensive knowledge of such interaction is thus fundamental to glycobiology. While the primary binding feature of GBPs can be easily uncovered by using a simple glycan microarray harboring limited numbers of glycan motifs, their fine specificities are harder to interpret. In this study, we prepared 98 closely related N-glycoforms that contain 5 common glycan epitopes which allowed the determination of the fine binding specificities of several plant lectins and anti-glycan antibodies. These N-glycoforms differ from each other at the monosaccharide level and were presented in an identical format to ensure comparability. With the analysis platform we used, it was found that most tested GBPs have preferences toward only one branch of the complex N-glycans, and their binding toward the epitope-presenting branch can be significantly affected by structures on the other branch. Fine specificities described here are valuable for a comprehensive understanding and applications of GBPs.

中文翻译：

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密切相关的糖型的微阵列分析揭示了 N-聚糖分支上聚糖决定簇的不同可及性。


聚糖通过聚糖结合蛋白 (GBP) 的识别来介导多种生物学作用。因此，对这种相互作用的全面了解是糖生物学的基础。虽然通过使用包含有限数量聚糖基序的简单聚糖微阵列可以轻松揭示 GBP 的主要结合特征，但它们的精细特异性更难以解释。在这项研究中，我们制备了 98 种密切相关的 N-糖型，其中包含 5 个常见的聚糖表位，从而可以确定几种植物凝集素和抗聚糖抗体的精细结合特异性。这些 N-糖型在单糖水平上彼此不同，并以相同的格式呈现以确保可比性。通过我们使用的分析平台，发现大多数测试的 GBP 仅对复杂 N-聚糖的一个分支有偏好，并且它们与表位呈递分支的结合可能会受到另一个分支上的结构的显着影响。这里描述的细节对于全面理解和应用 GBP 很有价值。