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A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: Individual patterns of reactivity in human sera

Identifieur interne : 004957 ( Main/Exploration ); précédent : 004956; suivant : 004958

A cluster of continuous antigenic structures in the transmembrane protein of HIV-1: Individual patterns of reactivity in human sera

Auteurs : Per Johan Klasse [Suède] ; Rüdiger Pipkorn [Allemagne] ; Jonas Blomberg [Suède]

Source :

RBID : ISTEX:3A459877F287EDB3547CC163578285BC0EB61AA9

Descripteurs français

English descriptors

Abstract

Abstract: We investigated the antigenicity of a highly conserved region in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1). In order to identify antigenically important residues, amino-acid sequences of synthetic peptides representing this region were varied systematically: single residues were omitted from the sequence of HIV-env 583–599; threonines were substituted for pairs of residues in HIV-env 581–599; the sequences of heptadeca-peptides were shifted by single residues. The peptides were tested in an enzyme immuno-assay against fourteen HIV-1 antibody-positive human sera, which were previously found to react with HIV-env 583–599, and against rabbit antisera to the peptides HIV-env 583–599 and 586–606. Substitutions as well as deletions in the sequence 589–596 (AVERYLKD) abrogated the antigenicity of the peptides with most of the human sera. Changes outside this sequence affected the reactivities differentially. Six overlapping dodeca-peptides, shifted in the sequence by single residues, lacked antigenicity in a competition assay, suggesting antigenic dependence on an ordered peptide conformation, which the longer peptides may preferentially assume. 19- and 21-mers with overlapping sequences competed to different extents with each other for binding to the antibodies of 3 human sera, illustrating that more than one antigenic structure in this narrow region can be recognized by a single polyclonal serum.

Url:
DOI: 10.1016/0161-5890(91)90130-C


Affiliations:


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<div type="abstract" xml:lang="en">Abstract: We investigated the antigenicity of a highly conserved region in the transmembrane protein of the human immunodeficiency virus type 1 (HIV-1). In order to identify antigenically important residues, amino-acid sequences of synthetic peptides representing this region were varied systematically: single residues were omitted from the sequence of HIV-env 583–599; threonines were substituted for pairs of residues in HIV-env 581–599; the sequences of heptadeca-peptides were shifted by single residues. The peptides were tested in an enzyme immuno-assay against fourteen HIV-1 antibody-positive human sera, which were previously found to react with HIV-env 583–599, and against rabbit antisera to the peptides HIV-env 583–599 and 586–606. Substitutions as well as deletions in the sequence 589–596 (AVERYLKD) abrogated the antigenicity of the peptides with most of the human sera. Changes outside this sequence affected the reactivities differentially. Six overlapping dodeca-peptides, shifted in the sequence by single residues, lacked antigenicity in a competition assay, suggesting antigenic dependence on an ordered peptide conformation, which the longer peptides may preferentially assume. 19- and 21-mers with overlapping sequences competed to different extents with each other for binding to the antibodies of 3 human sera, illustrating that more than one antigenic structure in this narrow region can be recognized by a single polyclonal serum.</div>
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