Departamento de Bioquímica e Biologia Molecular, Universidade Federal do Ceará, Fortaleza, Brazil.
Departamento de Bioquímica, Universidade Federal de Santa Catarina, Florianópolis, Brazil.
J Mol Recognit. 2020 Nov;33(11):e2870. doi: 10.1002/jmr.2870. Epub 2020 Jul 9.
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.
凝集素是一组非免疫来源的蛋白质，因其能够可逆地与碳水化合物结合而被识别。研究人员对寡糖和糖缀合物产生了兴趣，因为它们作为复杂细胞事件的介质，然后许多凝集素的生物技术应用是基于糖码解码及其活性。在这里，我们报告了一种来自 Canavalia bonariensis 种子的 ConA 样甘露糖/葡萄糖特异性凝集素 CaBo 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-甘露糖苷（M13）的结合，以及对急性炎症大鼠模型的体内影响。还进行了虚拟筛选，以涵盖 CaBo 可能的更多结合。计算机分析表明 CaBo 与甘露糖型配体的相互作用是稳定的，并且凝集素能够通过碳水化合物识别结构域（CRD）和组胺释放诱导大鼠急性炎症。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，支持了 CaBo 的生物学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。
