Molecular recognition remains one of the most desirable means of cellular communication. Each cell offers a unique surface pattern of biomolecules that makes it very specific about the nature of molecules that interact with the cell. Protein–glycan interaction has been one of the most common forms of cell signaling. Glycans expressed on the cell surface interact with an exogenous protein, and in many cases lead to a physiological response. These carbohydrate-binding proteins, commonly known as lectins, are very specific to the glycan they bind to. An exogenous lectin interacting with an animal cell surface glycan is generally studied using the classical hemagglutination assay. However, this method presents certain challenges that make it imperative to design and develop novel methods that are more specific and efficient in their interaction. In the last decade, a few methods have been developed to analyze more diverse reactions and use a lesser amount of sample. In some cases, the processing of the sample is also reduced. This review discusses how the methods have evolved over the decades and how they have reduced error while becoming more efficient.

中文翻译：

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研究碳水化合物-蛋白质相互作用的分析方法的演变简述

分子识别仍然是最理想的细胞通信方式之一。每个细胞都提供独特的生物分子表面图案，这使得与细胞相互作用的分子的性质非常具体。蛋白质-聚糖相互作用是细胞信号传导最常见的形式之一。细胞表面表达的聚糖与外源蛋白质相互作用，在许多情况下会导致生理反应。这些碳水化合物结合蛋白（通常称为凝集素）对其结合的聚糖具有很强的特异性。通常使用经典的血凝测定来研究与动物细胞表面聚糖相互作用的外源凝集素。然而，这种方法提出了某些挑战，因此必须设计和开发交互更加具体和高效的新颖方法。在过去的十年中，已经开发了一些方法来分析更多样化的反应并使用更少的样品。在某些情况下，样品的处理也会减少。这篇综述讨论了这些方法在过去几十年中是如何发展的，以及它们如何在提高效率的同时减少错误。