Role for the disulfide-bonded region of human immunodeficiency virus type 1 gp41 in receptor-triggered activation of membrane fusion function
Role for the disulfide-bonded region of human immunodeficiency virus type 1 gp41 in receptor-triggered activation of membrane fusion function
复制标题
DOI：
10.1016/j.bbrc.2010.03.071
复制
发表时间：
2010-04-16
影响因子：
3.1
通讯作者：
Poumbourios, Pantelis
中科院分区：
文献类型：
--
作者：
Bellamy-McIntyre, Anna K.;Baer, Severine;Poumbourios, Pantelis
人类免疫缺陷病毒 1 型 (HIV-1) 融合糖蛋白 gp41 的保守二硫键区域 (DSR) 介导与受体结合糖蛋白 gp120 的关联。 gp120、CD4 和趋化因子受体之间的相互作用激活 gp41 的融合活性。 HIV-1 (QH1549.13) DSR 中引入 W596L 和 W610F 突变可阻止病毒进入和半融合，而不影响 gp120-gp41 关联。融合缺陷与 CD4 触发的 gp41 前发夹形成的抑制相关，与 DSR 突变使 gp120 中受体诱导的构象变化与 gp41 激活解耦一致。我们的数据表明 DSR 感测 gp120-gp41 复合物中导致融合激活的构象变化。 (C) 2010 Elsevier Inc. 保留所有权利。
The conserved disulfide-bonded region (DSR) of the human immunodeficiency virus type 1 (HIV-1) fusion glycoprotein, gp41, mediates association with the receptor-binding glycoprotein, gp120. Interactions between gp120, CD4 and chemokine receptors activate the fusion activity of gp41. The introduction of W596L and W610F mutations to the DSR of HIV-1(QH1549.13) blocked viral entry and hemifusion without affecting gp120-gp41 association. The fusion defect correlated with inhibition of CD4-triggered gp41 pre-hairpin formation, consistent with the DSR mutations having decoupled receptor-induced conformational changes in gp120 from gp41 activation. Our data implicate the DSR in sensing conformational changes in the gp120-gp41 complex that lead to fusion activation. (C) 2010 Elsevier Inc. All rights reserved.