A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
A conserved HIV gp120 glycoprotein structure involved in chemokine receptor binding
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DOI：
10.1126/science.280.5371.1949
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发表时间：
1998-06-19
期刊：
影响因子：
56.9
通讯作者：
Sodroski, J
中科院分区：
文献类型：
--
作者：
Rizzuto, CD;Wyatt, R;Sodroski, J
灵长类免疫缺陷病毒进入靶细胞依赖于gp120包膜糖蛋白与细胞受体、CD4和趋化因子受体家族成员的顺序相互作用。gp120第三可变区（V3）环与趋化因子受体结合有关，但不同灵长类免疫缺陷病毒对CCR5趋化因子受体的使用表明涉及了另外的保守gp120元件。通过使用gp120突变体，显示高度保守的gp120结构对于CCR5结合是关键的。该结构位于V3环附近，并含有由CD4结合诱导的中和表位。该保守元件可能是人类免疫缺陷病毒（HIV）感染的药物或预防性干预的有用靶点。
The entry of primate immunodeficiency viruses into target cells depends on a sequential interaction of the gp120 envelope glycoprotein with the cellular receptors, CD4 and members of the chemokine receptor family. The gp120 third variable (V3) loop has been implicated in chemokine receptor binding, but the use of the CCR5 chemokine receptor by diverse primate immunodeficiency viruses suggests the involvement of an additional, conserved gp120 element. Through the use of gp120 mutants, a highly conserved gp120 structure was shown to be critical for CCR5 binding. This structure is located adjacent to the V3 loop and contains neutralization epitopes induced by CD4 binding. This conserved element may be a useful target for pharmacologic or prophylactic intervention in human immunodeficiency virus (HIV) infections.