Norrby E, Biberfeld G, Johnson P R, Parks D E, Houghten R A, Lerner R A
Department of Virology, Karolinska Institute, School of Medicine, Stockholm, Sweden.
AIDS Res Hum Retroviruses. 1989 Oct;5(5):487-93. doi: 10.1089/aid.1989.5.487.
The advent of site-directed serology has provided a specific and simplified means of distinguishing antibody responses to the two types of human immunodeficiency virus (HIV) in an outbred population. Remarkably, human sera containing HIV antibodies and simian sera containing simian immunodeficiency virus (SIV) antibodies had a very narrow amino acid dependence in the 23 residue long peptide, 582Ala-604Cys, used as antigen. A single dominating antigenic site was demonstrated in the C-terminal part of the peptide--596Trp-602Gln for HIV-2 and SIV antibodies and 597Gly-602Leu for HIV-1. A minor fraction of HIV-1 antibodies also reacted with a second site, 588Lys and 589Asp. These data define the precise amino acid dependence of a uniquely immunogenic site in the folded transmembrane protein of HIV and facilitate the optimizing of peptide antigens for site-directed serology.
位点特异性血清学的出现提供了一种在远交群体中区分针对两种人类免疫缺陷病毒（HIV）抗体反应的特异且简化的方法。值得注意的是，含有HIV抗体的人血清和含有猴免疫缺陷病毒（SIV）抗体的猴血清，在用作抗原的23个残基长的肽段（582Ala - 604Cys）中，氨基酸依赖性非常狭窄。在该肽段的C末端部分证实了一个主要的抗原位点——对于HIV - 2和SIV抗体为596Trp - 602Gln，对于HIV - 1为597Gly - 602Leu。一小部分HIV - 1抗体也与第二个位点（588Lys和589Asp）发生反应。这些数据确定了HIV折叠跨膜蛋白中一个独特免疫原性位点的精确氨基酸依赖性，并有助于优化用于位点特异性血清学的肽抗原。
