Moore J P, Sodroski J
Aaron Diamond AIDS Research Center, New York, New York 10016, USA.
J Virol. 1996 Mar;70(3):1863-72. doi: 10.1128/JVI.70.3.1863-1872.1996.
Forty-six monoclonal antibodies (MAbs) able to bind to the native, monomeric gp120 glycoprotein of the human immunodeficiency virus type 1 (HIV-1) LAI (HXBc2) strain were used to generate a competition matrix. The data suggest the existence of two faces of the gp120 glycoprotein. The binding sites for the viral receptor, CD4, and neutralizing MAbs appear to cluster on one face, which is presumably exposed on the assembled, oligomeric envelope glycoprotein complex. A second gp120 face, which is presumably inaccessible on the envelope glycoprotein complex, contains a number of epitopes for nonneutralizing antibodies. This analysis should be useful for understanding both the interaction of antibodies with the HIV-1 gp120 glycoprotein and neutralization of HIV-1.
46种能够与人免疫缺陷病毒1型(HIV-1)LAI(HXBc2)株天然单体gp120糖蛋白结合的单克隆抗体(MAb)被用于生成竞争矩阵。数据表明gp120糖蛋白存在两个面。病毒受体CD4和中和性单克隆抗体的结合位点似乎聚集在一个面上,这个面可能暴露在组装好的寡聚包膜糖蛋白复合物上。gp120的第二个面,可能在包膜糖蛋白复合物上无法接近,包含许多非中和性抗体的表位。该分析对于理解抗体与HIV-1 gp120糖蛋白的相互作用以及HIV-1的中和作用都应是有用的。