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CD4蛋白质是引起人类AIDS的HIV受体。为确定CD4与抗原提呈细胞表面相互作用以及与HIV相互作用的机理,作者分离并克隆了CD4基因,在几个不同的细胞中进行了该基因的表达。本文描述了有效表达系统,在该系统中重组并经过修剪的可溶性CD4(sCD4)被分泌到组织培养上清液中,24小时内能合成>3pg/ml的sCD4,培养4天以上的上清液中能提供近40mg/L的sCD_4。sCD4的纯度>95%,经纯化的sCD4仍保留在细胞表面CD4的结构和生物学特性。3ng的纯化sCD4足够能抑制100ng病毒蛋白质与细胞的结合。如果包膜糖蛋白是病毒总蛋白质的5%,CD4:gp110的比率为2:1时,能够完全抑制HIV结合到CD~+细胞。
The CD4 protein is the HIV receptor that causes human AIDS. To determine the mechanism by which CD4 interacts with antigen-presenting cells and interacts with HIV, the authors isolated and cloned the CD4 gene, which was expressed in several different cells. Described herein is an efficient expression system in which recombinant and pruned soluble CD4 (sCD4) is secreted into tissue culture supernatants and capable of synthesizing> 3 pg / ml sCD4 in 24 hours, supernatants cultured for more than 4 days Liquid can provide nearly 40mg / L sCD_4. The purity of sCD4 is> 95%. The purified sCD4 still retains the structural and biological characteristics of CD4 on the cell surface. 3 ng of purified sCD4 was sufficient to inhibit the binding of 100 ng of viral protein to the cells. If the envelope glycoprotein is 5% of the total viral protein, CD4: gp110 ratio of 2: 1, can completely inhibit HIV binding to CD ~ + cells.