Lectins are a group of proteins of non‐immune origin recognized for their ability to bind reversibly to carbohydrates. Researchers have been intrigued by oligosaccharides and glycoconjugates for their involvement as mediators of complex cellular events and then many biotechnological applications of lectins are based on glycocode decoding and their activities. Here, we report a structural and biological study of a ConA‐like mannose/glucose‐specific lectin from Canavalia bonariensis seeds, CaBo. More specifically, we evaluate the binding of CaBo with α‐methyl‐D‐mannoside (MMA) and mannose‐1,3‐α‐D‐mannose (M13) and the resultant in vivo effects on a rat model of acute inflammation. A virtual screening was also carried out to cover a larger number of possible bindings of CaBo. In silico analysis demonstrated the stability of CaBo interaction with mannose‐type ligands, and the lectin was able to induce acute inflammation in rats with the participation of the carbohydrate recognition domain (CRD) and histamine release. These results confirm the ability of CaBo to interact with hybrid and high‐mannose N‐glycans, supporting the hypothesis that CaBo's biological activity occurs primarily through its interaction with cell surface glycosylated receptors.

中文翻译：

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探索 Canavalia bonariensis 凝集素在炎症模型中的碳水化合物结合能力。

凝集素是一组非免疫来源的蛋白质，因其与碳水化合物可逆结合的能力而受到认可。研究人员对低聚糖和糖缀合物很感兴趣，因为它们作为复杂细胞事件的介质参与其中，然后凝集素的许多生物技术应用都基于糖代码解码及其活性。在这里，我们报告了来自Canavalia bonariensis种子 CaBo的类 ConA 甘露糖/葡萄糖特异性凝集素的结构和生物学研究。更具体地说，我们评估了 CaBo 与 α-甲基-D-甘露糖苷 (MMA) 和甘露糖-1,3-α-D-甘露糖 (M13) 的结合以及由此产生的对急性炎症大鼠模型的体内影响。还进行了虚拟筛选以覆盖更多可能的 CaBo 结合。计算机分析证明了 CaBo 与甘露糖型配体相互作用的稳定性，并且凝集素能够在碳水化合物识别域 (CRD) 和组胺释放的参与下诱导大鼠急性炎症。这些结果证实了 CaBo 与杂交和高甘露糖N-聚糖相互作用的能力，支持 CaBo 的生物活性主要通过与细胞表面糖基化受体相互作用发生的假设。