Lifson J, Coutré S, Huang E, Engleman E
J Exp Med. 1986 Dec 1;164(6):2101-6. doi: 10.1084/jem.164.6.2101.
Human immunodeficiency virus (HIV) envelope glycoprotein interactions with cell surface CD4 are involved in both virion infectivity and virally mediated cell fusion. D-mannose-specific lectins such as Con A specifically blocked virion infectivity and cell fusion. Studies with a recombinant vaccinia virus containing the HIV envelope gene demonstrated that Con A-mediated inhibition of HIV-induced fusion involved lectin binding to the viral envelope glycoprotein. These results indicate the importance of envelope glycosylation in the pathobiology of HIV infection, and suggest potential mechanisms for interfering with HIV infectivity and cytopathology.
人类免疫缺陷病毒（HIV）包膜糖蛋白与细胞表面CD4的相互作用参与了病毒体感染性和病毒介导的细胞融合过程。诸如伴刀豆球蛋白A（Con A）之类的D-甘露糖特异性凝集素可特异性阻断病毒体感染性和细胞融合。对含有HIV包膜基因的重组痘苗病毒的研究表明，Con A介导的对HIV诱导融合的抑制作用涉及凝集素与病毒包膜糖蛋白的结合。这些结果表明包膜糖基化在HIV感染发病机制中的重要性，并提示了干扰HIV感染性和细胞病变的潜在机制。
