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 : 004958A 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 :
- Molecular Immunology [ 0161-5890 ] ; 1991.
Descripteurs français
- KwdFr :
- Conformation moléculaire, Données de séquences moléculaires, Humains, Protéine d'enveloppe gp41 du VIH (immunologie), Sites de fixation des anticorps, Séquence d'acides aminés, Techniques immunoenzymatiques, Techniques in vitro, Thréonine (immunologie), VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie), Épitopes.
- MESH :
- immunologie : Protéine d'enveloppe gp41 du VIH, Thréonine, VIH-1 (Virus de l'Immunodéficience Humaine de type 1).
- Conformation moléculaire, Données de séquences moléculaires, Humains, Sites de fixation des anticorps, Séquence d'acides aminés, Techniques immunoenzymatiques, Techniques in vitro, Épitopes.
English descriptors
- KwdEn :
- MESH :
- chemical , immunology : HIV Envelope Protein gp41, Threonine.
- immunology : HIV-1.
- Teeft :
- Absorbance differences, Alpha helix, Amino, Amino Acid Sequence, Amino acid residues, Amino acids, Antibodies reactive, Antibody binding, Antigenic, Antigenic dependence, Antigenic structure, Antigenic structures, Antigenicity, Binding Sites, Antibody, Competition enzyme immunoassay, Deletion, Deletion peptides, Epitope, Epitopes, Helix, Human immunodeficiency virus, Human immunodeficiency virus type, Human sera, Human serum, Humans, Immune response, Immunodeficiency, Immunoenzyme Techniques, Immunosuppressive peptide, Important residues, In Vitro Techniques, Individual patterns, Johan klasse, Klasse, Lymphocyte proliferation, Medical microbiology, Microtitre plates, Middle column, Molecular Conformation, Molecular Sequence Data, Nucleotide sequence, Open triangles, Other parts, Peptide, Point mutation, Rabbit sera, Rabbit serum, Relative absorbance differences, Relative reactivities, Relative reactivity, Residue, Right column, Same peptide, Secondary structure, Serum, Serum polyspecificity, Short peptides, Side chains, Similar patterns, Single residues, Substitution, Synthetic peptide, Synthetic peptides, Threonine, Threonine substitutions, Titertek plates, Tobacco mosaic virus protein, Transmembrane, Transmembrane glycoprotein, Transmembrane protein, Unmodified peptides.
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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Le document en format XML
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<term>Binding Sites, Antibody</term>
<term>Epitopes</term>
<term>HIV Envelope Protein gp41 (immunology)</term>
<term>HIV-1 (immunology)</term>
<term>Humans</term>
<term>Immunoenzyme Techniques</term>
<term>In Vitro Techniques</term>
<term>Molecular Conformation</term>
<term>Molecular Sequence Data</term>
<term>Threonine (immunology)</term>
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<keywords scheme="KwdFr" xml:lang="fr"><term>Conformation moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Protéine d'enveloppe gp41 du VIH (immunologie)</term>
<term>Sites de fixation des anticorps</term>
<term>Séquence d'acides aminés</term>
<term>Techniques immunoenzymatiques</term>
<term>Techniques in vitro</term>
<term>Thréonine (immunologie)</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1) (immunologie)</term>
<term>Épitopes</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="immunology" xml:lang="en"><term>HIV Envelope Protein gp41</term>
<term>Threonine</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Protéine d'enveloppe gp41 du VIH</term>
<term>Thréonine</term>
<term>VIH-1 (Virus de l'Immunodéficience Humaine de type 1)</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en"><term>HIV-1</term>
</keywords>
<keywords scheme="Teeft" xml:lang="en"><term>Absorbance differences</term>
<term>Alpha helix</term>
<term>Amino</term>
<term>Amino Acid Sequence</term>
<term>Amino acid residues</term>
<term>Amino acids</term>
<term>Antibodies reactive</term>
<term>Antibody binding</term>
<term>Antigenic</term>
<term>Antigenic dependence</term>
<term>Antigenic structure</term>
<term>Antigenic structures</term>
<term>Antigenicity</term>
<term>Binding Sites, Antibody</term>
<term>Competition enzyme immunoassay</term>
<term>Deletion</term>
<term>Deletion peptides</term>
<term>Epitope</term>
<term>Epitopes</term>
<term>Helix</term>
<term>Human immunodeficiency virus</term>
<term>Human immunodeficiency virus type</term>
<term>Human sera</term>
<term>Human serum</term>
<term>Humans</term>
<term>Immune response</term>
<term>Immunodeficiency</term>
<term>Immunoenzyme Techniques</term>
<term>Immunosuppressive peptide</term>
<term>Important residues</term>
<term>In Vitro Techniques</term>
<term>Individual patterns</term>
<term>Johan klasse</term>
<term>Klasse</term>
<term>Lymphocyte proliferation</term>
<term>Medical microbiology</term>
<term>Microtitre plates</term>
<term>Middle column</term>
<term>Molecular Conformation</term>
<term>Molecular Sequence Data</term>
<term>Nucleotide sequence</term>
<term>Open triangles</term>
<term>Other parts</term>
<term>Peptide</term>
<term>Point mutation</term>
<term>Rabbit sera</term>
<term>Rabbit serum</term>
<term>Relative absorbance differences</term>
<term>Relative reactivities</term>
<term>Relative reactivity</term>
<term>Residue</term>
<term>Right column</term>
<term>Same peptide</term>
<term>Secondary structure</term>
<term>Serum</term>
<term>Serum polyspecificity</term>
<term>Short peptides</term>
<term>Side chains</term>
<term>Similar patterns</term>
<term>Single residues</term>
<term>Substitution</term>
<term>Synthetic peptide</term>
<term>Synthetic peptides</term>
<term>Threonine</term>
<term>Threonine substitutions</term>
<term>Titertek plates</term>
<term>Tobacco mosaic virus protein</term>
<term>Transmembrane</term>
<term>Transmembrane glycoprotein</term>
<term>Transmembrane protein</term>
<term>Unmodified peptides</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Conformation moléculaire</term>
<term>Données de séquences moléculaires</term>
<term>Humains</term>
<term>Sites de fixation des anticorps</term>
<term>Séquence d'acides aminés</term>
<term>Techniques immunoenzymatiques</term>
<term>Techniques in vitro</term>
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<front><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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