ROLE OF THE MATRIX PROTEIN IN THE VIRION ASSOCIATION OF THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEIN
ROLE OF THE MATRIX PROTEIN IN THE VIRION ASSOCIATION OF THE HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEIN
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DOI：
10.1128/jvi.68.3.1689-1696.1994
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发表时间：
1994-03-01
影响因子：
5.4
通讯作者：
GOTTLINGER, HG
中科院分区：
文献类型：
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作者：
DORFMAN, T;MAMMANO, F;GOTTLINGER, HG
人类免疫缺陷病毒1型（HIV-1）的基质（MA）蛋白直接在病毒体的脂质包膜下形成一层内被膜。衣壳周围的脂质包膜的外表面被病毒Env糖蛋白包被。我们在这里报告说，HIV-1包膜糖蛋白协会是非常敏感的MA蛋白的微小变化。结果表明，大多数的MA结构域的Gag前体，除了其羧基末端，是必不可少的这种协会。在编码MA蛋白的氨基末端100个氨基酸的区域中具有小错义或缺失突变的前病毒产生的病毒颗粒缺乏表面糖蛋白gp120和跨膜糖蛋白gp41，这表明在Env糖蛋白掺入水平上存在缺陷。MA结构域羧基末端的改变对颗粒相关的Env糖蛋白水平或病毒复制没有显著影响。HIV-1 MA蛋白序列的存在足以使HIV-1 Env糖蛋白与含有维斯纳病毒衣壳（CA）和核衣壳（NC）蛋白的杂合颗粒稳定缔合。HIV-1 Env糖蛋白与杂合颗粒的结合依赖于HIV-1 MA蛋白结构域的存在，因为当HIV-1 Env糖蛋白与真正的visna病毒Gag蛋白共表达时，不能有效地募集到病毒颗粒中。
The matrix (MA) protein of human immunodeficiency virus type 1 (HIV-1) forms an inner coat directly underneath the lipid envelope of the virion. The outer surface of the lipid envelope surrounding the capsid is coated by the viral Env glycoproteins. We report here that the HIV-1 capsid-Env glycoprotein association is very sensitive to minor alterations in the MA protein. The results indicate that most of the MA domain of the Gag precursor, except for its carboxy terminus, is essential for this association. Viral particles produced by proviruses with small missense or deletion mutations in the region coding for the amino-terminal 100 amino acids of the MA protein lacked both the surface glycoprotein gp120 and the transmembrane glycoprotein gp41, indicating a defect at the level of Env glycoprotein incorporation. Alterations at the carboxy terminus of the MA domain had no significant effect on the levels of particle-associated Env glycoprotein or on virus replication. The presence of HIV-1 MA protein sequences was sufficient for the stable association of HIV-1 Env glycoprotein with hybrid particles that contain the capsid (CA) and nucleocapsid (NC) proteins of visna virus. The association of HIV-1 Env glycoprotein with the hybrid particles was dependent upon the presence of the HIV-1 MA protein domain, as HIV-1 Env glycoprotein was not efficiently recruited into virus particles when coexpressed with authentic visna virus Gag proteins.