Secretion of a truncated form of the human immunodeficiency virus type 1 envelope glycoprotein.
Secretion of a truncated form of the human immunodeficiency virus type 1 envelope glycoprotein.
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人类免疫缺陷病毒 1 型包膜糖蛋白的截短形式的分泌。
DOI：
10.1006/viro.1993.1156
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发表时间：
1993
期刊：
影响因子：
3.7
通讯作者：
Compans,RW
中科院分区：
文献类型：
--
作者：
Hallenberger,S;Tucker,SP;Owens,RJ;Bernstein,HB;Compans,RW
我们已经鉴定了 HIV-1 包膜糖蛋白基因的截短分泌形式。通过重组牛痘病毒表达产生约 140 kDa (gp160t) 的糖蛋白产物和 120 kDa (gp120) 的少量裂解产物。脉冲追踪分析显示，大多数 gp160t 仍与细胞相关，并在合成后 10-20 小时内发生降解。合成后2-4小时在培养基中检测到分泌形式(gp160t/秒)和gp120，并且在20小时内没有显着降解。大多数细胞相关的 gp160t 对糖苷内切酶 H 的消化仍然敏感，而 gp160t/sec 和 gp120 在很大程度上具有抗性。 Gp160t、gp160t/sec 和 gp120 形成寡聚物，其通过分子间二硫键和/或非共价相互作用稳定，并且还发现与可溶性 CD4 结合。观察到野生型 gp160 和野生型 gp160t 在合成后 4-5 小时进行翻译后修饰，导致糖蛋白的电泳迁移率略有增加。用 N-糖苷酶 F 处理后，电泳迁移率的这些差异仍然存在，表明它们不是 N-连接寡糖加工的结果，但可能代表包膜糖蛋白的额外修饰。
We have characterized a truncated secreted form of the HIV-1 envelope glycoprotein gene. Expression via a recombinant vaccinia virus resulted in a glycoprotein product of approximately 140 kDa (gp160t) and a minor cleavage product of 120 kDa (gp120). Pulse-chase analysis revealed that the majority of gp160t remained cell-associated and underwent degradation within 10-20 hr of synthesis. A secreted form (gp160t/sec) and gp120 were detected in the media 2-4 hr postsynthesis and were not significantly degraded within a period of 20 hr. Most of the cell-associated gp160t remained sensitive to digestion with endoglycosidase H, whereas gp160t/sec and gp120 were largely resistant. Gp160t, gp160t/sec, and gp120 formed oligomers which were stabilized by intermolecular disulfide bonds and/or noncovalent interactions and were also found to bind to soluble CD4. Both wild type gp160 and wild type gp160t were observed to undergo a post-translational modification 4-5 hr postsynthesis, resulting in glycoproteins with a slightly increased electrophoretic mobility. These differences in electrophoretic mobility remained following treatment with N-glycosidase F, indicating that they are not a consequence of N-linked oligosaccharide processing, but may represent an additional modification of the envelope glycoprotein.