中和抗性和高感染性表型均由人类免疫缺陷病毒1型gp41亮氨酸拉链以及gp120受体和共受体结合域中相互作用残基的突变引起。
Both neutralization resistance and high infectivity phenotypes are caused by mutations of interacting residues in the human immunodeficiency virus type 1 gp41 leucine zipper and the gp120 receptor- and coreceptor-binding domains.
作者信息
Park E J, Quinnan G V
机构信息
Department of Preventive Medicine and Biometrics, Uniformed Services University of the Health Sciences, Bethesda, Maryland 20814, USA.
出版信息
J Virol. 1999 Jul;73(7):5707-13. doi: 10.1128/JVI.73.7.5707-5713.1999.
Abstract
Neutralization resistance of human immunodeficiency virus type 1 (HIV-1) is a major impediment to vaccine development. We have found that residues of HIV-1 MN strain in the C terminus of gp120 and the leucine zipper (LZ) region of gp41 viral envelope proteins interact cooperatively to determine neutralization resistance and modulate infectivity. Further, results demonstrate that this interaction, by which regions of gp120 are assembled onto the LZ, involves amino acid residues intimately related to those which participate in the binding of the envelope to its receptor and coreceptor. Variations in this critical assembly structure determine the concordant, interdependent evolution of increased infectivity efficiency and neutralization resistance phenotypes of the envelopes. The results elucidate important structure-function relationships among epitopes that are important targets of vaccine development.
摘要
1型人类免疫缺陷病毒（HIV-1）的中和抗性是疫苗开发的主要障碍。我们发现，gp120 C末端的HIV-1 MN株残基与gp41病毒包膜蛋白的亮氨酸拉链（LZ）区域协同相互作用，以确定中和抗性并调节感染性。此外，结果表明，这种gp120区域组装到LZ上的相互作用涉及与参与包膜与其受体和共受体结合的氨基酸残基密切相关的氨基酸残基。这种关键组装结构的变化决定了包膜的感染效率增加和中和抗性表型的一致、相互依赖的进化。这些结果阐明了作为疫苗开发重要靶点的表位之间重要的结构-功能关系。
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