Characterization of a neutralizing monoclonal antibody to the external glycoprotein of HIV-1.
Characterization of a neutralizing monoclonal antibody to the external glycoprotein of HIV-1.
复制标题
针对 HIV-1 外部糖蛋白的中和单克隆抗体的表征。
DOI：
10.1159/000150266
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发表时间：
1992
期刊：
影响因子：
4.6
通讯作者：
Sarngadharan,MG
中科院分区：
文献类型：
--
作者：
Pal,R;diMarzoVeronese,F;Nair,BC;Rahman,R;Hoke,G;Mumbauer,SW;Sarngadharan,MG
HIV-1的外部糖蛋白上的主要中和表位进行了研究，与HIV-1蛋白的抗体，这两者都能够中和病毒的感染性的抗体阳性的人血清的单克隆抗体和。该单克隆抗体与HIV-1 IIIB的gp 120特异性反应，并被证明能中和CEM细胞被无细胞病毒体感染，并抑制通常在未感染细胞与HIV-1感染细胞共培养时观察到的合胞体的形成。HIV-1抗体阳性人血清也证明了类似的病毒感染中和和合胞体形成抑制。通过检查来自已知含有中和表位的HIV-1 gp 120区域的许多重叠肽，该表位位于外部糖蛋白分子中的氨基酸307和320（V3环）之间。单克隆抗体不干扰gpl 20与CD 4的结合，或不干扰CD 4诱导的gpl 20从病毒包膜脱落的后续步骤。然而，它阻断了凝血酶对V3环的蛋白水解裂解，表明该抗体可能抑制该环与其他膜结合蛋白的相互作用。
The major neutralizing epitope on the external glycoprotein of HIV-1 was studied with an envelope-specific monoclonal antibody and with a human serum positive for antibodies to HIV-1 proteins, both of which were able to neutralize virus infectivity. The monoclonal antibody reacted specifically with gp120 from HIV-1IIIB, and was shown to neutralize infection of CEM cells by cell-free virions, and inhibited the formation of syncytia normally observed when uninfected cells are cocultured with HIV-1-infected cells. Similar neutralization of viral infection and inhibition of syncytia formation was also demonstrated by the HIV-1-antibody-positive human serum. By examining a number of overlapping peptides from a region of HIV-1 gpl20 known to contain a neutralizing epitope, this epitope was localized between amino acids 307 and 320 (V3 loop) in the external glycoprotein molecule. The monoclonal antibody did not interfere with the binding of gpl20 to CD4, or with the subsequent step of CD4-induced shedding of gpl20 from the viral envelope. However, it blocked the proteolytic cleavage of the V3 loop by thrombin, suggesting that the antibody may be inhibiting the interaction of the loop with other membrane-bound proteins.