Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120
Structural basis of tyrosine sulfation and VH-gene usage in antibodies that recognize the HIV type 1 coreceptor-binding site on gp120
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DOI：
10.1073/pnas.0308527100
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发表时间：
2004-03-02
影响因子：
11.1
通讯作者：
Kwong, PD
中科院分区：
文献类型：
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作者：
Huang, CC;Venturi, M;Kwong, PD
HIV-1 gp 120包膜糖蛋白结合HIV-1辅助受体的保守表面被多层伪装保护而不被体液识别。在这里，我们提出的序列和基因组分析12抗体，穿透这些防御，并确定晶体结构的5。这些数据揭示了三种不寻常的免疫特征的机制和原子水平的细节：通过抗体的酪氨酸硫酸化对辅助受体的翻译后模拟，控制这种硫酸化的另一种分子机制，以及高度选择性的V-H基因使用。当面对非同寻常的病毒防御时，免疫系统展现出新的适应能力，酪氨酸硫酸化增强了抗原识别的词汇。
The conserved surface of the HIV-1 gp120 envelope glycoprotein that binds to the HIV-1 coreceptor is protected from humoral recognition by multiple layers of camouflage. Here we present sequence and genomic analyses for 12 antibodies that pierce these defenses and determine the crystal structures of 5. The data reveal mechanisms and atomic-level details for three unusual immune features: posttranslational mimicry of coreceptor by tyrosine sulfation of antibody, an alternative molecular mechanism controlling such sulfation, and highly selective V-H-gene usage. When confronted by extraordinary viral defenses, the immune system unveils novel adaptive capabilities, with tyrosine sulfation enhancing the vocabulary of antigen recognition.