Novel Fold and Carbohydrate Specificity of the Potent Anti-HIV Cyanobacterial Lectin from Oscillatoria agardhii
Novel Fold and Carbohydrate Specificity of the Potent Anti-HIV Cyanobacterial Lectin from Oscillatoria agardhii
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DOI：
10.1074/jbc.m110.173278
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发表时间：
2011-01-14
影响因子：
4.8
通讯作者：
Gronenborn, Angela M.
中科院分区：
文献类型：
--
作者：
Koharudin, Leonardus M. I.;Furey, William;Gronenborn, Angela M.
琼脂颤藻凝集素（OAA）是近年来发现的一种具有抗HIV活性的蓝藻凝集素。到目前为止，只有其一级结构和碳水化合物结合数据。为了阐明OAA的抗病毒机制的结构基础，我们确定了这种凝集素的结构，通过X-射线晶体学在1.2埃的分辨率和映射的特定碳水化合物识别位点的OAA的NMR光谱。OAA的整体结构包括10条β链，折叠成单个紧凑的β桶状结构域，与蛋白质数据库中所有已知的蛋白质结构相比，形成了独特的拓扑结构。针对Man-9和Man-9的各种二糖组分测试OAA糖结合。两个对称的碳水化合物结合位点位于蛋白质上，并发现Manalpha（1-6）Man-linked糖的偏好。总之，我们的结构结果解释了OAA的抗病毒活性，并增加了越来越多的关于抗病毒凝集素的知识。
Oscillatoria agardhii agglutinin (OAA) is a recently discovered cyanobacterial lectin that exhibits potent anti-HIV activity. Up to now, only its primary structure and carbohydrate binding data have been available. To elucidate the structural basis for the antiviral mechanism of OAA, we determined the structure of this lectin by x-ray crystallography at 1.2 angstrom resolution and mapped the specific carbohydrate recognition sites of OAA by NMR spectroscopy. The overall architecture of OAA comprises 10 beta-strands that fold into a single, compact, beta-barrel-like domain, creating a unique topology compared with all known protein structures in the Protein Data Bank. OAA sugar binding was tested against Man-9 and various disaccharide components of Man-9. Two symmetric carbohydrate-binding sites were located on the protein, and a preference for Man alpha(1-6) Man-linked sugars was found. Altogether, our structural results explain the antiviral activity OAA and add to the growing body of knowledge about antiviral lectins.