感染猴体内中和抗体所识别的猿猴-人类免疫缺陷病毒包膜糖蛋白表位的特性分析
Characterization of simian-human immunodeficiency virus envelope glycoprotein epitopes recognized by neutralizing antibodies from infected monkeys.
作者信息
Etemad-Moghadam B, Karlsson G B, Halloran M, Sun Y, Schenten D, Fernandes M, Letvin N L, Sodroski J
机构信息
Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts, USA.
出版信息
J Virol. 1998 Oct;72(10):8437-45. doi: 10.1128/JVI.72.10.8437-8445.1998.
Abstract
We characterized human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein epitopes recognized by neutralizing antibodies from monkeys recently infected by molecularly cloned simian-human immunodeficiency virus (SHIV) variants. The early neutralizing antibody response in each infected animal was directed mainly against a single epitope. This primary neutralizing epitope, however, differed among individual monkeys infected by identical viruses. Two such neutralization epitopes were determined by sequences in the V2 and V3 loops of the gp120 envelope glycoprotein, while a third neutralization epitope, apparently discontinuous, was determined by both V2 and V3 sequences. These results indicate that the early neutralizing antibody response in SHIV-infected monkeys is monospecific and directed against epitopes composed of the gp120 V2 and V3 variable loops.
摘要
我们对被分子克隆的猿猴-人类免疫缺陷病毒（SHIV）变体近期感染的猴子体内中和抗体所识别的人类免疫缺陷病毒1型（HIV-1）包膜糖蛋白表位进行了特性分析。每只受感染动物早期的中和抗体反应主要针对单个表位。然而，在被相同病毒感染的个体猴子中，这种主要的中和表位有所不同。两个这样的中和表位由gp120包膜糖蛋白的V2和V3环中的序列决定，而第三个中和表位显然是不连续的，由V2和V3序列共同决定。这些结果表明，SHIV感染的猴子中早期的中和抗体反应是单特异性的，且针对由gp120 V2和V3可变环组成的表位。
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