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The antigenic structure of the HIV gp120 envelope glycoprotein (see comments)

机译：HIV gp120包膜糖蛋白的抗原结构（请参阅评论）

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摘要

The human immunodeficiency virus HIV-1 establishes persistent infections in humans which lead to acquired immunodeficiency syndrome (AIDS). The HIV-1 envelope glycoproteins, gp120 and gp41, are assembled into a trimeric complex that mediates virus entry into target cells. HIV-1 entry depends on the sequential interaction of the gp120 exterior envelope glycoprotein with the receptors on the cell, CD4 and members of the chemokine receptor family. The gp120 glycoprotein, which can be shed from the envelope complex, elicits both virus-neutralizing and non-neutralizing antibodies during natural infection. Antibodies that lack neutralizing activity are often directed against the gp120 regions that are occluded on the assembled trimer and which are exposed only upon shedding. Neutralizing antibodies, by contrast, must access the functional envelope glycoprotein complex and typically recognize conserved or variable epitopes near the receptor-binding regions. Here we describe the spatial organization of conserved neutralization epitopes on gp120, using epitope maps in conjunction with the X-ray crystal structure of a ternary complex that includes a gp120 core, CD4 and a neutralizing antibody. A large fraction of the predicted accessible surface of gp120 in the trimer is composed of variable, heavily glycosylated core and loop structures that surround the receptor-binding regions. Understanding the structural basis for the ability of HIV-1 to evade the humoral immune response should assist in the design of a vaccine.
机译：人类免疫缺陷病毒HIV-1在人类中建立了持续性感染，从而导致获得性免疫缺陷综合症（AIDS）。 HIV-1包膜糖蛋白gp120和gp41被组装成三聚体复合物，介导病毒进入靶细胞。 HIV-1的进入取决于gp120外膜糖蛋白与细胞，CD4受体和趋化因子受体家族成员的顺序相互作用。可以从包膜复合物中脱落的gp120糖蛋白在自然感染过程中同时引起病毒中和性和非中和性抗体。缺乏中和活性的抗体通常直接针对被封闭在三聚体上的gp120区域，这些区域仅在脱落时才暴露。相比之下，中和抗体必须接近功能性包膜糖蛋白复合物，并且通常识别受体结合区附近的保守或可变表位。在这里，我们使用表位图结合包括gp120核心，CD4和中和抗体的三元复合物的X射线晶体结构，描述了gp120上保守的中和表位的空间组织。三聚体中gp120的预计可及表面的很大一部分由围绕受体结合区的可变的，高度糖基化的核心和环结构组成。了解HIV-1逃避体液免疫反应能力的结构基础应有助于疫苗的设计。

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