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人类免疫缺陷病毒跨膜糖蛋白中免疫显性结构域的精细定位

Fine mapping of an immunodominant domain in the transmembrane glycoprotein of human immunodeficiency virus.

作者信息

Gnann J W, Nelson J A, Oldstone M B

出版信息

J Virol. 1987 Aug;61(8):2639-41. doi: 10.1128/JVI.61.8.2639-2641.1987.

DOI:10.1128/JVI.61.8.2639-2641.1987
PMID:2439707
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC255715/
Abstract

Sera from virtually all individuals infected with human immunodeficiency virus contain antibodies against the viral envelope glycoproteins. By using a series of synthetic peptide antigens, we identified an immunodominant domain at amino acid position 598-609 of gp41. The minimal essential epitope is a 7-amino-acid sequence (amino acids 603-609) containing two cysteine residues. Both cysteine residues are required for the antigenic conformation of the sequence, possibly due to creation of a cyclic structure via disulfide bond formation.

摘要

几乎所有感染人类免疫缺陷病毒的个体血清中都含有针对病毒包膜糖蛋白的抗体。通过使用一系列合成肽抗原,我们在gp41的氨基酸位置598 - 609处鉴定出一个免疫显性结构域。最小必需表位是一个包含两个半胱氨酸残基的7氨基酸序列(氨基酸603 - 609)。这两个半胱氨酸残基对于该序列的抗原构象都是必需的,可能是由于通过二硫键形成产生了环状结构。

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