*Department of Chemistry and Biochemistry, Arizona State University, Tempe, AZ 85287, U.S.A.
Biochem Soc Trans. 2013 Oct;41(5):1170-6. doi: 10.1042/BST20130154.
CVN (cyanovirin-N), a small lectin isolated from cyanobacteria, exemplifies a novel class of anti-HIV agents that act by binding to the highly glycosylated envelope protein gp120 (glycoprotein 120), resulting in inhibition of the crucial viral entry step. In the present review, we summarize recent work in our laboratory and others towards determining the crucial role of multivalency in the antiviral activity, and we discuss features that contribute to the high specificity and affinity for the glycan ligand observed in CVN. An integrated approach that encompasses structural determination, mutagenesis analysis and computational work holds particular promise to clarify aspects of the interactions between CVN and glycans.
CVN（氰基病毒素-N）是一种从小型蓝藻中分离出来的凝集素，它是一种新型抗 HIV 药物，通过与高度糖基化的包膜蛋白 gp120（糖蛋白 120）结合来抑制关键的病毒进入步骤。在本综述中，我们总结了我们实验室和其他实验室最近的工作，这些工作旨在确定多价性在抗病毒活性中的关键作用，并讨论了导致 CVN 对聚糖配体具有高特异性和亲和力的特征。一种综合的方法，包括结构测定、突变分析和计算工作，有望澄清 CVN 与聚糖之间相互作用的各个方面。
