Structure and polymorphism of HIV-1 third variable loops
Structure and polymorphism of HIV-1 third variable loops
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DOI：
10.1074/jbc.271.14.8236
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发表时间：
1996-04-05
影响因子：
4.8
通讯作者：
Gupta, G
中科院分区：
文献类型：
--
作者：
Catasti, P;Bradbury, EM;Gupta, G
HIV-1表面糖蛋白gp 120的第三可变环（V3）一直是中和抗体的靶点，然而，V3环内的序列变异降低了其作为抗HIV-1的潜在疫苗的有效性，V3环结构的难以捉摸的性质促使我们对不同的分离株进行系统的研究，试图鉴定V3环中的共同结构基序，我们以前已经确定了两个V3环的结构特征：V3泰国和V3 RIN，在本文中，我们提出了另外两个变体的结构：V3海地和V3 RF。我们的结果表明，在所有四个V3环中观察到相似的二级结构：中和结构域中心的GPG（R/K/Q）峰、中心峰侧翼的两个延伸区域和C-末端结构域中的螺旋区域。对于Haitian V3环，我们还展示了保守的结构特征是如何通过编码在C-氨基酸序列中的构象开关被掩盖的。GPGK波峰的终端侧。
The third variable (V3) loop of HIV-1 surface glycoprotein, gp120, has been the target of neutralizing antibodies, However, sequence variation inside the V3 loop diminishes its effectiveness as a potential vaccine against HIV-1, The elusive nature of the V3 loop structure prompted us to carry out a systematic study on different isolates in an attempt to identify a common structural motif in the V3 loop regardless of the amino acid sequence variability, We have previously determined the structural features of two V3 loops: V3 Thailand and V3 RIN, In this paper, we present the structure of two other variants: V3 Haiti and V3 RF. Our results show that similar secondary structures are observed in all the four V3 loops: a GPG(R/K/Q) crest in the center of the neutralizing domain, two extended regions flanking the central crest, and a helical region in the C-terminal domain, For the Haitian V3 loop, we also show how the conserved structural features are masked through a conformational switch encoded in the amino acid sequences on the C-terminal side of the GPGK crest.