Department of Chemistry, Georgia State University, Atlanta, GA 30303, USA.
Department of Chemistry, University of California, One Shields Avenue, Davis, CA, 95616, USA.
Glycobiology. 2020 Apr 20;30(5):334-345. doi: 10.1093/glycob/cwz100.
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.
糖链通过与糖结合蛋白（GBP）的识别来介导多种生物学功能。因此，全面了解这种相互作用对于糖生物学至关重要。虽然使用含有有限数量糖基基序的简单糖芯片可以轻松揭示 GBP 的主要结合特征，但它们的精细特异性更难解释。在这项研究中，我们制备了 98 种密切相关的 N-糖型，它们包含 5 种常见的糖表位，这使得能够确定几种植物凝集素和抗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，并以相同的形式呈现，以确保可比性。使用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，并且它们对表位呈现分支的结合可以受到另一个分支上结构的显著影响。这里描述的精细特异性对于全面理解和应用 GBP 非常有价值。
