Evaluation of structure-antigenicity relationship of peptides from human immunodeficiency virus type 1 (HIV-1) p18 protein by circular dichroism
Identifieur interne : 000367 ( France/Analysis ); précédent : 000366; suivant : 000368Evaluation of structure-antigenicity relationship of peptides from human immunodeficiency virus type 1 (HIV-1) p18 protein by circular dichroism
Auteurs : Kamel Mabrouk [France] ; Maxime Moulard [France] ; Jean Claude Gluckman [France] ; Régine Romi [France] ; Hervé Rochat [France] ; Jurphaas Van Rietschoten [France] ; Elmostafa Bahraoui [France]Source :
- Molecular Immunology [ 0161-5890 ] ; 1993.
English descriptors
- Teeft :
- Agence nationale, Aids disease, Amino acid, Amino acid sequences, Antibodies reactive, Antigenic, Antigenic activity, Antigenic determinants, Antigenic regions, Antigenicity, Aqueous solution, Cell epitopes, Cell recognition, Central region, Chimpanzee, Chimpanzee sera, Circular dichroism, Conformation, Conformational equilibrium, Core protein, Cyclic peptide, Denatured form, Dichroism, Dimensional structure, Disease virus, Elisa reactivity, Entire sequence, Epitope, Epitope mapping, Feline immunodeficiency virus, Fine specificity, Helper epitopes, Human immunodeficiency virus, Human immunodeficiency virus type, Human sera, Immun, Immunodeficiency, Immunodominant region, Immunosorbent assay, Kamel mabrouk, Large peptides, Long peptide, Long peptides, Monoclonal antibodies, More antigenic, Mouse mabs, Native protein, Peptide, Positive sera, Possible correlation, Reactive, Recent data, Saccharomyces cerevisiae, Same line, Secondary structure, Secondary structures, Short ones, Short peptide, Short peptides, Similar observations, Solid phase peptide synthesis, Structural analysis, Synthetic peptide, Synthetic peptides, Viral, Wahren.
Abstract
Abstract: The antigenicity of Human Immunodeficiency Virus type 1 (HIV-1) matrix p18 protein was evaluated by analyzing the specificity of anti-p18 antibodies elicited either in HIV-1 infected humans, or in HIV-1 infected or immunized chimpanzees, against a panel of long and short overlapping synthetic peptides [from 12 to 46 amino acid (aa) residues] covering the entire sequence of p18. The relationship between peptide structure and antigenicity was further investigated by probing the secondary structures of the peptides by circular dichroism. The results obtained clearly showed the immunodominance of the N-terminal region mimicked by peptide P1 (aa 2-45), which reacted with 52 and 100% of human and chimpanzee anti-p18 sera, respectively. In contrast smaller 15 aa long peptides C1, C2, C3, C4 and P3 which cover the entire sequence of immunodominant peptide P1, showed only weak or no reactivity. In contrast to widely accepted hypotheses, circular dichroism analysis of both small and large peptides secondary structures did not show any obvious correlation between antigenicity and the ability of peptides to adopt an ordered conformation.
Url:
DOI: 10.1016/0161-5890(93)90118-U
Affiliations:
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de Biochimie CNRS URA 1455, Faculté de Médecine Nord, Bd Pierre Dramard, 13326 Marseille cédex 15</wicri:regionArea><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille cédex 15</settlement></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j">Molecular Immunology</title><title level="j" type="abbrev">MIMM</title><idno type="ISSN">0161-5890</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1993">1993</date><biblScope unit="volume">30</biblScope><biblScope unit="issue">5</biblScope><biblScope unit="page" from="503">503</biblScope><biblScope unit="page" to="512">512</biblScope></imprint><idno type="ISSN">0161-5890</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0161-5890</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Agence nationale</term><term>Aids disease</term><term>Amino acid</term><term>Amino acid sequences</term><term>Antibodies reactive</term><term>Antigenic</term><term>Antigenic activity</term><term>Antigenic determinants</term><term>Antigenic regions</term><term>Antigenicity</term><term>Aqueous solution</term><term>Cell epitopes</term><term>Cell recognition</term><term>Central region</term><term>Chimpanzee</term><term>Chimpanzee sera</term><term>Circular dichroism</term><term>Conformation</term><term>Conformational equilibrium</term><term>Core protein</term><term>Cyclic peptide</term><term>Denatured form</term><term>Dichroism</term><term>Dimensional structure</term><term>Disease virus</term><term>Elisa reactivity</term><term>Entire sequence</term><term>Epitope</term><term>Epitope mapping</term><term>Feline immunodeficiency virus</term><term>Fine specificity</term><term>Helper epitopes</term><term>Human immunodeficiency virus</term><term>Human immunodeficiency virus type</term><term>Human sera</term><term>Immun</term><term>Immunodeficiency</term><term>Immunodominant region</term><term>Immunosorbent assay</term><term>Kamel mabrouk</term><term>Large peptides</term><term>Long peptide</term><term>Long peptides</term><term>Monoclonal antibodies</term><term>More antigenic</term><term>Mouse mabs</term><term>Native protein</term><term>Peptide</term><term>Positive sera</term><term>Possible correlation</term><term>Reactive</term><term>Recent data</term><term>Saccharomyces cerevisiae</term><term>Same line</term><term>Secondary structure</term><term>Secondary structures</term><term>Short ones</term><term>Short peptide</term><term>Short peptides</term><term>Similar observations</term><term>Solid phase peptide synthesis</term><term>Structural analysis</term><term>Synthetic peptide</term><term>Synthetic peptides</term><term>Viral</term><term>Wahren</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: The antigenicity of Human Immunodeficiency Virus type 1 (HIV-1) matrix p18 protein was evaluated by analyzing the specificity of anti-p18 antibodies elicited either in HIV-1 infected humans, or in HIV-1 infected or immunized chimpanzees, against a panel of long and short overlapping synthetic peptides [from 12 to 46 amino acid (aa) residues] covering the entire sequence of p18. The relationship between peptide structure and antigenicity was further investigated by probing the secondary structures of the peptides by circular dichroism. The results obtained clearly showed the immunodominance of the N-terminal region mimicked by peptide P1 (aa 2-45), which reacted with 52 and 100% of human and chimpanzee anti-p18 sera, respectively. In contrast smaller 15 aa long peptides C1, C2, C3, C4 and P3 which cover the entire sequence of immunodominant peptide P1, showed only weak or no reactivity. In contrast to widely accepted hypotheses, circular dichroism analysis of both small and large peptides secondary structures did not show any obvious correlation between antigenicity and the ability of peptides to adopt an ordered conformation.</div></front></TEI><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li><li>Île-de-France</li></region><settlement><li>Marseille cédex 15</li><li>Paris cédex 13</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Mabrouk, Kamel" sort="Mabrouk, Kamel" uniqKey="Mabrouk K" first="Kamel" last="Mabrouk">Kamel Mabrouk</name></region><name sortKey="Bahraoui, Elmostafa" sort="Bahraoui, Elmostafa" uniqKey="Bahraoui E" first="Elmostafa" last="Bahraoui">Elmostafa Bahraoui</name><name sortKey="Gluckman, Jean Claude" sort="Gluckman, Jean Claude" uniqKey="Gluckman J" first="Jean Claude" last="Gluckman">Jean Claude Gluckman</name><name sortKey="Moulard, Maxime" sort="Moulard, Maxime" uniqKey="Moulard M" first="Maxime" last="Moulard">Maxime Moulard</name><name sortKey="Rochat, Herve" sort="Rochat, Herve" uniqKey="Rochat H" first="Hervé" last="Rochat">Hervé Rochat</name><name sortKey="Romi, Regine" sort="Romi, Regine" uniqKey="Romi R" first="Régine" last="Romi">Régine Romi</name><name sortKey="Van Rietschoten, Jurphaas" sort="Van Rietschoten, Jurphaas" uniqKey="Van Rietschoten J" first="Jurphaas" last="Van Rietschoten">Jurphaas Van Rietschoten</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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