Recognition Properties of V3-Specific Antibodies to V3 Loop Peptides Derived from HIV-1 gp120 Presented in Multiple Conformations†
Identifieur interne : 003645 ( Main/Curation ); précédent : 003644; suivant : 003646Recognition Properties of V3-Specific Antibodies to V3 Loop Peptides Derived from HIV-1 gp120 Presented in Multiple Conformations†
Auteurs : J. G. Huisman [Pays-Bas] ; A. Carotenuto [Pays-Bas] ; A. F. Labrijn [Pays-Bas] ; C. H. M. Papavoine [Pays-Bas] ; J. D. Laman [Pays-Bas] ; M. M. Schellekens [Pays-Bas] ; M. H. G. M. Koppelman [Pays-Bas] ; C. W. Hilbers [Pays-Bas]Source :
- Biochemistry [ 0006-2960 ] ; 2000.
Abstract
To identify structural constraints and amino acid sequences important for antibody recognition of the third variable domain (V3) of HIV-1 gp120, we have studied the solution conformation of three 35-mer circular V3 loop peptides derived from HIV-1 strains which differ in syncytium- (SI) and non-syncytium-inducing (NSI) capacity. In addition to 2D NMR and CD analyses, fluid- and solid-phase immunoassays were performed using V3-specific antibodies to V3 peptides and gp120 derived from different strains of HIV-1. NMR and CD spectroscopy indicated that circular and linear V3 loops exist in water as a dynamic ensemble of multiple conformations. Amino acid substitutions and biochemical modifications of the V3 loop were found to affect antibody binding depending on the presentation of the antigens. From NMR observations and immunological experiments, we provide evidence for a V3 loop specific monoclonal antibody interaction which is directed predominantly against linear epitopes rather than against discontinuous epitopes. The absence of a single defined solution conformation of 35-mer circular V3 peptides should be taken into account when using V3-related peptides to investigate structural elements in the V3 domain of the gp120 envelope protein of HIV-1 involved in biological processes of the virus.
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DOI: 10.1021/bi0004504
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Carotenuto</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation><affiliation></affiliation></author><author><name sortKey="Labrijn, A F" sort="Labrijn, A F" uniqKey="Labrijn A" first="A. F." last="Labrijn">A. F. Labrijn</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation></author><author><name sortKey="Papavoine, C H M" sort="Papavoine, C H M" uniqKey="Papavoine C" first="C. H. M." last="Papavoine">C. H. M. Papavoine</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation><affiliation></affiliation></author><author><name sortKey="Laman, J D" sort="Laman, J D" uniqKey="Laman J" first="J. D." last="Laman">J. D. Laman</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation><affiliation></affiliation></author><author><name sortKey="Schellekens, M M" sort="Schellekens, M M" uniqKey="Schellekens M" first="M. M." last="Schellekens">M. M. Schellekens</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation></author><author><name sortKey="Koppelman, M H G M" sort="Koppelman, M H G M" uniqKey="Koppelman M" first="M. H. G. M." last="Koppelman">M. H. G. M. Koppelman</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation></author><author><name sortKey="Hilbers, C W" sort="Hilbers, C W" uniqKey="Hilbers C" first="C. W." last="Hilbers">C. W. Hilbers</name><affiliation wicri:level="3"><country xml:lang="fr">Pays-Bas</country><wicri:regionArea>CLB, Sanquin Blood Supply Foundation, Laboratory for Clinical and Experimental Immunology, Department ofPathophysiology of Plasma Proteins, Amsterdam, The Netherlands, NSR Center for Molecular Structure, Design and Synthesis,Laboratory of Biophysical Chemistry, University of Nijmegen, Nijmegen, The Netherlands, Department of Biochemistry andBiophysics, University of Gothenburg, Gothenburg, Sweden, EUR, Department of Immunology, Rotterdam, The Netherlands,and TNO Prevention and Health, Division of Immunological and Infectious Diseases, Leiden</wicri:regionArea><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation><affiliation></affiliation><affiliation wicri:level="1"><country wicri:rule="url">Pays-Bas</country><wicri:regionArea> Correspondence should be addressed to this author at the NSRCenter for Molecular Structure, Design and Synthesis, Laboratory ofBiophysical Chemistry, University of Nijmegen, Toernooiveld 1, 6525ED Nijmegen</wicri:regionArea><placeName><settlement type="city">Nimègue</settlement><region type="province" nuts="2">Gueldre</region></placeName></affiliation></author></analytic><monogr></monogr><series><title level="j" type="main">Biochemistry</title><title level="j" type="abbrev">Biochemistry</title><idno type="ISSN">0006-2960</idno><idno type="eISSN">1520-4995</idno><imprint><publisher>American Chemical Society</publisher><date type="e-published">2000</date><date type="published">2000</date><biblScope unit="vol">39</biblScope><biblScope unit="issue">35</biblScope><biblScope unit="page" from="10866">10866</biblScope><biblScope unit="page" to="10876">10876</biblScope></imprint><idno type="ISSN">0006-2960</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0006-2960</idno></seriesStmt></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract">To identify structural constraints and amino acid sequences important for antibody recognition of the third variable domain (V3) of HIV-1 gp120, we have studied the solution conformation of three 35-mer circular V3 loop peptides derived from HIV-1 strains which differ in syncytium- (SI) and non-syncytium-inducing (NSI) capacity. In addition to 2D NMR and CD analyses, fluid- and solid-phase immunoassays were performed using V3-specific antibodies to V3 peptides and gp120 derived from different strains of HIV-1. NMR and CD spectroscopy indicated that circular and linear V3 loops exist in water as a dynamic ensemble of multiple conformations. Amino acid substitutions and biochemical modifications of the V3 loop were found to affect antibody binding depending on the presentation of the antigens. From NMR observations and immunological experiments, we provide evidence for a V3 loop specific monoclonal antibody interaction which is directed predominantly against linear epitopes rather than against discontinuous epitopes. The absence of a single defined solution conformation of 35-mer circular V3 peptides should be taken into account when using V3-related peptides to investigate structural elements in the V3 domain of the gp120 envelope protein of HIV-1 involved in biological processes of the virus.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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