Part of the C-terminal tall of the envelope gp41 transmembrane glycoprotein of human immunodeficiency virus type 1 is exposed on the surface of infected cells and is involved in virus-mediated cell fusion
Part of the C-terminal tall of the envelope gp41 transmembrane glycoprotein of human immunodeficiency virus type 1 is exposed on the surface of infected cells and is involved in virus-mediated cell fusion
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DOI：
10.1099/vir.0.80439-0
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发表时间：
2005-01-01
影响因子：
3.8
通讯作者：
Dimmock, NJ
中科院分区：
文献类型：
--
作者：
Cheung, L;McLain, L;Dimmock, NJ
人类免疫缺陷病毒1型（HIV-1）病毒粒子的GP41跨膜糖蛋白的C末端通常被认为是在病毒体内的，但最近已显示，该尾巴的一部分暴露在病毒体外部。在这里，使用一系列抗体，证明尾巴的同一部分暴露在HIV-1感染的C8166淋巴母细胞的表面上，并被表达GP41的疫苗感染的HELA细胞。病毒重组。两种类型的感染细胞都无法与P117基质蛋白特异性IgG反应，直到用皂苷透化，从而证实了质膜的完整性。 GP41尾部的细胞表面暴露是通过一种GP41尾巴特异性抗体抑制HIV-1介导的细胞融合的独立证明的。这些数据还暗示了在病毒融合过程中直接或间接地或间接的GP41 C末端尾部的暴露区域。它的表面暴露表明GP41 C末端尾巴可能是免疫干预或感染化疗的候选者。
The C-terminal tail of the gp41 transmembrane glycoprotein of the human immunodeficiency virus type 1 (HIV-1) virion is usually thought to be inside the virion, but it has been shown recently that part of the tail is exposed on the virion exterior. Here, using a panel of antibodies, it was demonstrated that the same part of the tail is exposed on the surface of HIV-1-infected C8166 lymphoblastoid cells and HeLa cells infected with a gp41-expressing vaccinia. virus recombinant. Both types of infected cell failed to react with p117 matrix protein-specific IgGs until permeabilized with saponin, confirming the integrity of the plasma membrane. Cell-surface exposure of the gp41 tail was independently demonstrated by inhibition of HIV-1-mediated cell-cell fusion by one of the gp41 tail-specific antibodies. These data also implicate the exposed region of the gp41 C-terminal tail either directly or indirectly in the viral fusion process. Its surface exposure suggests that the gp41 C-terminal tail may be a candidate for immune intervention or chemotherapy of infection.