MYRISTOYLATION-DEPENDENT REPLICATION AND ASSEMBLY OF HUMAN IMMUNODEFICIENCY VIRUS-1
MYRISTOYLATION-DEPENDENT REPLICATION AND ASSEMBLY OF HUMAN IMMUNODEFICIENCY VIRUS-1
复制标题
DOI：
10.1073/pnas.87.2.523
复制
发表时间：
1990-01-01
影响因子：
11.1
通讯作者：
RATNER, L
中科院分区：
文献类型：
--
作者：
BRYANT, M;RATNER, L
肉豆蔻酸与 Pr55gag 的 N 端甘氨酸残基共价连接，Pr55gag 是人类免疫缺陷病毒 1 (HIV-1) 主要结构蛋白的前体，促进了病毒组装和传播的重要步骤。在 HIV-1 的功能性克隆中，用丙氨酸取代肉豆蔻酰基受体甘氨酸，可以消除病毒复制。反式地补充这种缺陷可以恢复感染性颗粒的产生。非肉豆蔻酰化 (myr-) gag 前体在受感染细胞中积累，并且不会加工成完整病毒颗粒的成熟衣壳成分。然而，myr-Pr55gag 可以在体外被纯化的 HIV 蛋白酶加工，这表明肉豆蔻酰基部分不是蛋白酶切割所必需的。 Pr55gag 的肉豆蔻酰化不是定位所必需的，但它是 HIV-1 膜稳定结合和组装所必需的。
Covalent linkage of myristic acid to the N-terminal glycine residue to Pr55gag, the precursor of the major structural proteins of human immunodeficiency virus 1 (HIV-1), facilitates an essential step in virus assembly and propagation. Substitution of the myristoyl-acceptor glycine with alanine, in a functional clone of HIV-1, eliminates virus replication. Complementation of this defect, in trans, restores infectious particle production. The nonmyristoylated (myr-) gag precursor accumulates in infected cells and is not processed into the mature capsid components of the intact virion. However, myr- Pr55gag can be processes by purified HIV protease in vitro, demonstrating that the myristoyl moiety is not required for cleavage by the protease. Myristoylation of Pr55gag is not necessary for localization but it required for stable membrane association and assembly of HIV-1.