Epitopes at the Proteolytic Cleavage Sites of HIV-1-gp120 and RSV-F Protein Share a Sequence Homology: Comparative Studies with Virus-Induced and Antipeptide Antibodies
作者:
Hans-Jürgen Streckert,
Hermann Werchau,
期刊:
Intervirology
(Karger Available online 1992)
卷期:
Volume 34,
issue 1
页码: 30-37
ISSN:0300-5526
年代: 1992
DOI:10.1159/000150260
出版商: S. Karger AG
关键词: HIV;Respiratory syncytial virus;Synthetic peptides;Proteolytic cleavage
数据来源: Karger
摘要:
The proteolytic cleavage sites of the human immunodeficiency virus type 1 (HIV-1) envelope glycoprotein precursor gpl60 and the fusion protein of respiratory syncytial virus (RSV) show a sequence homology. To study this homology two synthetic peptides corresponding to HIV-1-env-gpl60-aa 507–518 (KAKRRWQREKR) and RSV-F2-aa 130–136 (SKKRKRR) were synthesized. Human serum samples from HIV-positive or RSV-positive collections recognized the appropriate peptide in 90.6 or 37.2% respectively. No cross-reactivity towards the non-homologous peptide could be monitored in both serum collections. In contrast, antipeptide antibodies raised against both peptides demonstrate a high degree of cross-reactivity. These data indicate that the high specificity of the virus-induced antibodies may be a result of strong conformational restrictions at the proteolytic cleavage site of both proteins. Moreover, these observations are important for diagnostic purposes. Synthetic peptides are a valuable tool for HIV antibody screening. Our data provide information concerning the specificity of antigen-antibody interaction on a highly immunogenic HIV-1 epit
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