EFFECTS OF DELETIONS IN THE CYTOPLASMIC DOMAIN ON BIOLOGICAL FUNCTIONS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEINS
EFFECTS OF DELETIONS IN THE CYTOPLASMIC DOMAIN ON BIOLOGICAL FUNCTIONS OF HUMAN-IMMUNODEFICIENCY-VIRUS TYPE-1 ENVELOPE GLYCOPROTEINS
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DOI：
10.1128/jvi.66.6.3306-3315.1992
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发表时间：
1992-06-01
影响因子：
5.4
通讯作者：
SODROSKI, J
中科院分区：
文献类型：
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作者：
GABUZDA, DH;LEVER, A;SODROSKI, J
研究了人类免疫缺陷病毒1型(HIV-1)包膜糖蛋白胞质结构域在病毒复制中的作用。Gp41羧基末端840至856位残基的缺失降低了病毒在CD4结合和DNA前病毒形成之间的早期阶段的病毒进入效率，而不影响包膜糖蛋白的合成、加工或合胞体形成能力。846位氨基酸残基的缺失与COS-1细胞产生的包膜糖蛋白的稳定性降低有关，但这种表型与细胞类型有关。将HIV-1包膜糖蛋白掺入病毒粒子中不需要gp41的胞质结构域。这些结果表明，gp41胞浆结构域的羧基末端在HIV-1进入过程中发挥了作用，而不是受体结合或膜融合。在某些细胞类型中，gp41的胞质结构域也影响包膜糖蛋白的稳定性。
The role of the cytoplasmic domain of the human immunodeficiency virus type 1 (HIV-1) envelope glycoproteins in virus replication was investigated. Deletion of residues 840 to 856 at the carboxyl terminus of gp41 reduced the efficiency of virus entry during an early step in the virus life cycle between CD4 binding and formation of the DNA provirus without affecting envelope glycoprotein synthesis, processing, or syncytium-forming ability. Deletion of residues amino terminal to residue 846 was associated with decreased stability of envelope glycoproteins made in COS-1 cells, but this phenotype was cell type dependent. The cytoplasmic domain of gp41 was not required for the incorporation of the HIV-1 envelope glycoproteins into virions. These results suggest that the carboxyl terminus of the gp41 cytoplasmic domain plays a role in HIV-1 entry other than receptor binding or membrane fusion. The cytoplasmic domain of gp41 also affects the stability of the envelope glycoprotein in some cell types.