A defined conformational epitope from the C4 domain of HIV type 1 glycoprotein 120: anti-cyclic C4 antibodies from HIV-positive donors magnify glycoprotein 120 suppression of interleukin 2 produced by T cells.
A defined conformational epitope from the C4 domain of HIV type 1 glycoprotein 120: anti-cyclic C4 antibodies from HIV-positive donors magnify glycoprotein 120 suppression of interleukin 2 produced by T cells.
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来自 HIV 1 型糖蛋白 120 的 C4 结构域的明确构象表位：来自 HIV 阳性供体的抗环 C4 抗体可放大糖蛋白 120 对 T 细胞产生的白细胞介素 2 的抑制。
DOI：
10.1089/08892220151126625
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发表时间：
2001
影响因子：
1.5
通讯作者：
Robert-Guroff,M
中科院分区：
文献类型：
--
作者：
Robey,FA;Robert-Guroff,M
HIV gp120的C4结构域在gp120与靶细胞上的CD4受体结合的过程中起着至关重要的作用。从免疫的兔和HIV阳性的人的血清中获得了针对11个氨基酸的环状C4多肽的抗体，并发现它们能识别与CD4结合的gp120。抗循环C4抗体可在体外放大gp120对T细胞产生的IL-2的抑制作用。兔抗11个氨基酸的线性C4多肽的抗体不识别游离态或与CD4结合时的gp120。这些结果表明，gp120C4区域的一个构象定义的、高度保守的表位仍然暴露在CD4结合上。天然产生的针对该表位的抗体可以增强gp120诱导的免疫抑制，并可能有助于疾病的进展。
The C4 domain of HIV gp120 plays a functionally vital role in the binding of gp120 to CD4 receptors on target cells. Antibodies to an 11-amino acid cyclic C4 peptide were obtained from immunized rabbits and from the serum of an HIV-positive human and were found to recognize gp120 bound to CD4. Anti-cyclic C4 antibodies magnified gp120-induced suppression of IL-2 produced by T cellsin vitro. Rabbit antibodies to the 11-amino acid linear C4 peptide did not recognize gp120 in the free state or when bound to CD4. These results indicate that a conformationally defined, highly conserved epitope in the gp120 C4 region remains exposed on CD4 binding. Naturally occurring antibodies to this epitope can augment gp120-induced immunosuppression and may contribute to disease progression.