Synthetic peptides and anti-peptide antibodies as probes to study interdomain interactions involved in virus assembly: the envelope of the human immunodeficiency virus (HIV-1).
Synthetic peptides and anti-peptide antibodies as probes to study interdomain interactions involved in virus assembly: the envelope of the human immunodeficiency virus (HIV-1).
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合成肽和抗肽抗体作为探针来研究病毒组装中涉及的域间相互作用：人类免疫缺陷病毒 (HIV-1) 的包膜。
DOI：
10.1016/0042-6822(92)90729-9
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发表时间：
1992
期刊：
影响因子：
3.7
通讯作者：
Jiang,S
中科院分区：
文献类型：
--
作者：
Neurath,AR;Strick,N;Jiang,S
合成肽和抗肽抗体已被广泛用作探针以定位蛋白质上的B细胞和T细胞表位。这样的探针还具有描绘通常涉及蛋白质-蛋白质相互作用或蛋白质内结构域缔合的接触位点的潜力。我们应用肽/抗肽探针来定义：（1）人类免疫缺陷病毒1型（HIV-1）包膜糖蛋白gp 120和gp 41上参与这两种糖蛋白之间结合的区域;（2）gp 120/gp 41上HIV-1与CD 4细胞受体结合所必需的位点。（1）gp 120上的两个区段，包括残基（102-126）和（425-452），有助于CD 4的结合位点，并且预期在折叠的gp 120链中并置;（2）分别包括残基（303-338）和（579-611）的免疫显性gp 120和gp 41表位的部分似乎参与gp 120-gp 41缔合，正如直接结合研究和HIV-1病毒粒子上这些表位的有限可及性所表明的：gp 120的其他部分似乎也有助于这两种糖蛋白之间的结合;（3）gp 120上gp 41和CD 4结合位点之间存在部分重叠;（4）gp 41的融合结构域和片段（637-666）在gp 41寡聚化后不能被抗体接近;（5）gp 120-gp 41结合被金精三羧酸阻断，这表明开发干扰HIV-1组装的抗病毒化合物的可能性。
Synthetic peptides and anti-peptide antibodies have been widely used as probes to map B- and T-cell epitopes on proteins. Such probes also have the potential to delineate contact sites involved generally in protein-protein interactions or in association of domains within a protein. We applied peptide/anti-peptide probes to define: (1) regions on the human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins gp120 and gp41 involved in the association between these two glycoproteins; and (2) sites on gp120/gp41, essential for the association of HIV-1 with the CD4 cell receptor. Results of this examination suggested the following: (1) two segments on gpl20, encompassing residues (102–126) and (425–452), contribute to the binding site for CD4 and are expected to be juxtaposed in the folded gp120 chain; (2) portions of immunodominant gpl20 and gp41 epitopes, encompassing residues (303–338) and (579–611), respectively, appeared to be involved in the gpl20-gp41 association, as suggested by direct binding studies and by the limited accessibility of these epitopes on HIV-1 virions: other portions of gp120 also appeared to contribute to the association between these two glycoproteins; (3) there is a partial overlap between gp41 and CD4 binding sites on gp120; (4) the fusion domain and a segment (637–666) of gp41 are not accessible to antibodies after oligomerization of gp41; and (5) the gp120-gp41 association was blocked by aurintricarboxylic acid, suggesting the possibility of developing antiviral compounds interfering with HIV-1 assembly.