ROLE OF INTRACELLULAR TRAFFIC IN HIV INFECTION

人类免疫缺陷病毒的T细胞受体CD4依赖于 糖基化以获得适当的表面表达。初步研究采用 急性淋巴细胞性白血病细胞扩增成功 含CD4CDNA的重组质粒转入突变体和野生型 中国仓鼠卵巢细胞类型。对这些克隆人的描述表明 表明CD4含有双天线未唾液酸化的复合型寡糖。 数据还表明，CD4无法到达细胞表面 当它缺乏碳水化合物是由于选择性地降解 去糖基化的CD4。 HIV的Rev蛋白最近被证明会导致早产儿 编码包膜糖蛋白的部分剪接信使核糖核酸的转运 从细胞核到细胞质。开发一个系统来检查 REV效应，一种在体外产生核的方法已经被设计出来 异乎寻常地添加了DNA。这种方法涉及到使用 非洲爪哇在那里已经证明了核组装可以 重新组合。这种制剂的供应应允许 REV作用机制的研究。在其他研究中，考试 已经开始研究核孔复合体的结构，Rev， Tat和其他病毒蛋白在病毒感染后发生交叉。这个 利用重组DNA技术研究了孔道复合体的结构。 主要的核孔糖蛋白np62已被克隆、测序和 在培养的细胞中表达。编码这种蛋白质的基因一直是 发现该基因全长2.95kb，不含内含子。这个 这种蛋白质初级序列的可获得性使得 与p62反应的抗肽抗体的制备。这些 抗体对于探测毛孔复合体的功能应该是有用的。 在艾滋病毒的生命周期中。

CD4, the T-cell receptor for the human immunodeficiency virus, depends upon glycosylation for proper surface expression. Initial studies employing acute lymphoblastic leukemic cells were extended by the successful transfection of a plasmid containing the CDNA for CD4 into mutant and wild type Chinese hamster ovary cells. Characterization of these clones suggests that CD4 contains biantennary unsialylated complex-type oligosaccharides. The data also suggest that the inability of CD4 to reach the cell surface when it lacks carbohydrate is due to the selective degradation of unglycosylated CD4. The REV protein of HIV has been recently shown to lead to the premature transport of the partially spliced MRNA encoding the envelope glycoprotein from the nucleus to the cytoplasm. To develop a.system to examine the effects of REV, a means has been devised for generating nuclei in vitro around exogously added DNA. This method involves using extracts from Xenopus laevis where it has been demonstrated that nuclear assembly can be reconstituted. The availability of such preparations should allow examination of the mechanism of REV function. In other studies, examination has begun of the structure of the nuclear pore complex, across which REV, TAT, and other viral proteins cross following viral infection. The structure of the pore complex is explored using recombinant DNA techniques. The major nuclear pore glycoprotein np62 has been cloned, sequenced and expressed in cultured cells. The gene encoding this protein has been isolated and found to be 2.95 kb in length and devoid of introns. The availability of the primary sequence of this protein has allowed the preparation of anti-peptide antibodies which react with p62. These antibodies should prove useful for probing the function of the pore complex in the HIV life cycle.