MAP OF SEQUENTIAL B-CELL EPITOPES OF THE HIV-1 TRANSMEMBRANE PROTEIN USING HUMAN-ANTIBODIES AS PROBE
MAP OF SEQUENTIAL B-CELL EPITOPES OF THE HIV-1 TRANSMEMBRANE PROTEIN USING HUMAN-ANTIBODIES AS PROBE
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DOI:
10.1159/000150169
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发表时间:
1990-11-01
期刊:
影响因子:
4.6
通讯作者:
BRASSEUR, R
中科院分区:
文献类型:
--
作者:
GOUDSMIT, J;MELOEN, RH;BRASSEUR, R
Antibodies of individuals infected with the human immunodeficiency virus type 1 (HIV-1) were used to probe the antigenicity of the HIV-1 transmembrane protein of 41 kD (gp41) by antibody-reactive peptide scanning (Pepscan). Eleven distinct sequential antibody-binding sites were defined by testing reactivity to 339 overlapping nonapeptides spanning the complete gp41 amino acid sequence. Such analysis only maps continuous antibody-binding sites of nine amino acids in length and does not identify putative discontinuous or assembled epitopes. Three B cell epitopes (aa 609-622; aa 655-699; aa 664-681) at the amino-terminal border of the putative transmembrane anchor and two (aa 732-748; aa 744-762) at the carboxyl-terminal border of this domain were the most antigenic. One antibody-binding domain (aa 834-852) with four amino acids homologous to the beta-1 domain of HLA class II beta-chain was recognized by the serum in 1 of 4 AIDS patients tested and not by any of the eight sera from symptom-free individuals. Although functional domains of gp41 involved in virus replication, cytopathicity and possibly immunossuppression were shown to bind antibodies of HIV-1-infected individuals, no relationship between antibody recognition patterns and disease progression was apparent.