Cross-comparison of Protein Recognition of Sialic Acid Diversity on Two Novel Sialoglycan Microarrays
Cross-comparison of Protein Recognition of Sialic Acid Diversity on Two Novel Sialoglycan Microarrays
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DOI：
10.1074/jbc.m112.359323
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发表时间：
2012-06-29
影响因子：
4.8
通讯作者：
Varki, Ajit
中科院分区：
文献类型：
--
作者：
Padler-Karavani, Vered;Song, Xuezheng;Varki, Ajit
DNA 和蛋白质阵列被普遍认为是研究中强大的探索工具。这主要是通过建立适当的质量控制指南来实现的，允许不同阵列平台之间的交叉比较。作为自然延伸，随后开发了聚糖微阵列，并且使用此类阵列的最新进展极大地增强了我们对自然界中蛋白质-聚糖识别的理解。然而，尽管假设具有生物学意义的蛋白质-聚糖结合可以通过聚糖微阵列可靠地检测到，但用于产生、呈现、偶联和检测聚糖的方法存在很大差异，并且缺乏系统的交叉比较。我们通过比较两个阵列来解决这些问题，这两个阵列一起代表了自然界中唾液酸修饰、连接和潜在聚糖的显着多样性，包括一些相同的基序。我们比较和对比了与各种已知和新型植物、脊椎动物和病毒唾液酸识别蛋白的结合相互作用，并提出了利用唾液酸链的轻度高碘酸盐氧化来评估特异性的技术进展。这些数据证明了唾液酸的多样性和聚糖阵列的分析能力，表明不同格式的不同呈现提供了聚糖结合蛋白特异性的有用且互补的解释。他们还强调了聚糖阵列技术未来的重要挑战和问题，并表明不能简单地假设具有相似聚糖结构的聚糖阵列会给出相似的结果。
DNA and protein arrays are commonly accepted as powerful exploratory tools in research. This has mainly been achieved by the establishment of proper guidelines for quality control, allowing cross-comparison between different array platforms. As a natural extension, glycan microarrays were subsequently developed, and recent advances using such arrays have greatly enhanced our understanding of protein-glycan recognition in nature. However, although it is assumed that biologically significant protein-glycan binding is robustly detected by glycan microarrays, there are wide variations in the methods used to produce, present, couple, and detect glycans, and systematic cross-comparisons are lacking. We address these issues by comparing two arrays that together represent the marked diversity of sialic acid modifications, linkages, and underlying glycans in nature, including some identical motifs. We compare and contrast binding interactions with various known and novel plant, vertebrate, and viral sialic acid-recognizing proteins and present a technical advance for assessing specificity using mild periodate oxidation of the sialic acid chain. These data demonstrate both the diversity of sialic acids and the analytical power of glycan arrays, showing that different presentations in different formats provide useful and complementary interpretations of glycan-binding protein specificity. They also highlight important challenges and questions for the future of glycan array technology and suggest that glycan arrays with similar glycan structures cannot be simply assumed to give similar results.