Anti-V3 and anti-IgG antibodies of healthy individuals share complementarity structures
It was recently shown that antibodies reactive with a peptide from the tip of the HIV-1NY5 gp120 V3 loop (V3 peptide) are present not only in sera of HIV-positive patients but also in sera of healthy HIV-negative individuals. In the present study, we show that V3 peptide reactive antibodies are pred...
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Veröffentlicht in: | Journal of acquired immune deficiency syndromes (1999) 1999-08, Vol.21 (4), p.266-270 |
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description | It was recently shown that antibodies reactive with a peptide from the tip of the HIV-1NY5 gp120 V3 loop (V3 peptide) are present not only in sera of HIV-positive patients but also in sera of healthy HIV-negative individuals. In the present study, we show that V3 peptide reactive antibodies are predominantly IgM in sera of HIV negative individuals and that a fraction of the IgG anti-V3 antibodies exhibit features of autoantibodies. These antibodies were purified by chromatography on IgG-sepharose columns from sera as well as from purified IgG anti-V3 antibodies. A higher IgG anti-V3 reactivity was detected in autoantibody preparations from HIV-positive sera as compared with the reactivity of sera and purified antibodies from HIV-negative individuals. This was confirmed by solid phase binding of IgG anti-V3 antibodies both to V3 and to human IgG F(ab')2 antigens. The autoantibodies did not bind to peptides that share sequence similarity with V3 peptide indicating a high epitope specificity. The detection of antibodies against HIV epitopes in HIV-negative individuals may suggest that anti-V3 antibodies after HIV infection represent at least in part a secondary immune response. |
doi_str_mv | 10.1097/00126334-199908010-00002 |
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In the present study, we show that V3 peptide reactive antibodies are predominantly IgM in sera of HIV negative individuals and that a fraction of the IgG anti-V3 antibodies exhibit features of autoantibodies. These antibodies were purified by chromatography on IgG-sepharose columns from sera as well as from purified IgG anti-V3 antibodies. A higher IgG anti-V3 reactivity was detected in autoantibody preparations from HIV-positive sera as compared with the reactivity of sera and purified antibodies from HIV-negative individuals. This was confirmed by solid phase binding of IgG anti-V3 antibodies both to V3 and to human IgG F(ab')2 antigens. The autoantibodies did not bind to peptides that share sequence similarity with V3 peptide indicating a high epitope specificity. The detection of antibodies against HIV epitopes in HIV-negative individuals may suggest that anti-V3 antibodies after HIV infection represent at least in part a secondary immune response.</description><identifier>ISSN: 1077-9450</identifier><identifier>ISSN: 1525-4135</identifier><identifier>EISSN: 2331-6993</identifier><identifier>EISSN: 1944-7884</identifier><identifier>DOI: 10.1097/00126334-199908010-00002</identifier><identifier>PMID: 10428103</identifier><identifier>CODEN: JDSRET</identifier><language>eng</language><publisher>New York, NY: Raven Press</publisher><subject>AIDS/HIV ; Analysis of the immune response. Humoral and cellular immunity ; Antibodies, Anti-Idiotypic - blood ; Antibodies, Anti-Idiotypic - chemistry ; Antibody Affinity ; Autoantibodies - blood ; Autoantibodies - chemistry ; Biological and medical sciences ; Cell interactions ; Cross Reactions ; Fundamental and applied biological sciences. Psychology ; Fundamental immunology ; HIV ; HIV Antibodies - blood ; HIV Antibodies - chemistry ; HIV Envelope Protein gp120 - immunology ; HIV Seronegativity - immunology ; HIV Seropositivity - immunology ; Human immunodeficiency virus ; Human viral diseases ; Humans ; Immunobiology ; Immunoglobulin G - blood ; Immunoglobulin G - chemistry ; Immunoglobulin G - immunology ; Immunoglobulin M - blood ; Immunoglobulin M - chemistry ; Immunoglobulin Variable Region - blood ; Immunoglobulin Variable Region - chemistry ; Immunology ; Infectious diseases ; Medical sciences ; Peptide Fragments - immunology ; Peptides ; Viral diseases ; Viral diseases of the lymphoid tissue and the blood. 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In the present study, we show that V3 peptide reactive antibodies are predominantly IgM in sera of HIV negative individuals and that a fraction of the IgG anti-V3 antibodies exhibit features of autoantibodies. These antibodies were purified by chromatography on IgG-sepharose columns from sera as well as from purified IgG anti-V3 antibodies. A higher IgG anti-V3 reactivity was detected in autoantibody preparations from HIV-positive sera as compared with the reactivity of sera and purified antibodies from HIV-negative individuals. This was confirmed by solid phase binding of IgG anti-V3 antibodies both to V3 and to human IgG F(ab')2 antigens. The autoantibodies did not bind to peptides that share sequence similarity with V3 peptide indicating a high epitope specificity. The detection of antibodies against HIV epitopes in HIV-negative individuals may suggest that anti-V3 antibodies after HIV infection represent at least in part a secondary immune response.</description><subject>AIDS/HIV</subject><subject>Analysis of the immune response. Humoral and cellular immunity</subject><subject>Antibodies, Anti-Idiotypic - blood</subject><subject>Antibodies, Anti-Idiotypic - chemistry</subject><subject>Antibody Affinity</subject><subject>Autoantibodies - blood</subject><subject>Autoantibodies - chemistry</subject><subject>Biological and medical sciences</subject><subject>Cell interactions</subject><subject>Cross Reactions</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>HIV</subject><subject>HIV Antibodies - blood</subject><subject>HIV Antibodies - chemistry</subject><subject>HIV Envelope Protein gp120 - immunology</subject><subject>HIV Seronegativity - immunology</subject><subject>HIV Seropositivity - immunology</subject><subject>Human immunodeficiency virus</subject><subject>Human viral diseases</subject><subject>Humans</subject><subject>Immunobiology</subject><subject>Immunoglobulin G - blood</subject><subject>Immunoglobulin G - chemistry</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunoglobulin M - blood</subject><subject>Immunoglobulin M - chemistry</subject><subject>Immunoglobulin Variable Region - blood</subject><subject>Immunoglobulin Variable Region - chemistry</subject><subject>Immunology</subject><subject>Infectious diseases</subject><subject>Medical sciences</subject><subject>Peptide Fragments - immunology</subject><subject>Peptides</subject><subject>Viral diseases</subject><subject>Viral diseases of the lymphoid tissue and the blood. Aids</subject><issn>1077-9450</issn><issn>1525-4135</issn><issn>2331-6993</issn><issn>1944-7884</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkE1r3DAQhkVpaTZp_0IxpfTmdOSx19IxhHxBoJfQHsVYGnUV_LGV7MD--yjZbRMiGDSH5x1eHiEKCacSdPsDQFZrxLqUWmtQIKGE_Kp3YlUhynKtNb4XKwltW-q6gSNxnNJ9TrWI8FEcSagrJQFX4vfZOIfyFxY0ujx5v_lz9bx0kwuciskXG6Z-3uyKMLrwENxCfSrShiIXdhq2PQ88zhTDvCvSHBc7L5HTJ_HBZ44_H_4TcXd5cXd-Xd7-vLo5P7stbS3buSSZ21tQHZDyznvvwErskCnXI3YWSWPjmBpPTWdVxRq9VNg5bRkIT8T3_dltnP4unGYzhGS572nkaUnmSQS2GjL49Q14Py1xzNVMNrZualQqQ2oP2TilFNmbbQwDxZ2RYJ7Em3_izX_x5ll8jn453F-6gd2r4N50Br4dAEqWeh9ptCG9cEqpul3jI6OsjBQ</recordid><startdate>19990801</startdate><enddate>19990801</enddate><creator>METLAS, R</creator><creator>TRAJKOVIC, D</creator><creator>SRDIC, T</creator><creator>VELJKOVIC, V</creator><creator>COLOMBATTI, A</creator><general>Raven Press</general><general>Lippincott Williams & Wilkins Ovid Technologies</general><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7T2</scope><scope>7T5</scope><scope>7TK</scope><scope>7U7</scope><scope>7U9</scope><scope>C1K</scope><scope>H94</scope><scope>K9.</scope><scope>7X8</scope></search><sort><creationdate>19990801</creationdate><title>Anti-V3 and anti-IgG antibodies of healthy individuals share complementarity structures</title><author>METLAS, R ; TRAJKOVIC, D ; SRDIC, T ; VELJKOVIC, V ; COLOMBATTI, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c417t-a1080c08b0a8fdfffd0c13b3ea810aedc3a935dea5fa5bc82e93f183bd9ce0a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>AIDS/HIV</topic><topic>Analysis of the immune response. Humoral and cellular immunity</topic><topic>Antibodies, Anti-Idiotypic - blood</topic><topic>Antibodies, Anti-Idiotypic - chemistry</topic><topic>Antibody Affinity</topic><topic>Autoantibodies - blood</topic><topic>Autoantibodies - chemistry</topic><topic>Biological and medical sciences</topic><topic>Cell interactions</topic><topic>Cross Reactions</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>HIV</topic><topic>HIV Antibodies - blood</topic><topic>HIV Antibodies - chemistry</topic><topic>HIV Envelope Protein gp120 - immunology</topic><topic>HIV Seronegativity - immunology</topic><topic>HIV Seropositivity - immunology</topic><topic>Human immunodeficiency virus</topic><topic>Human viral diseases</topic><topic>Humans</topic><topic>Immunobiology</topic><topic>Immunoglobulin G - blood</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunoglobulin M - blood</topic><topic>Immunoglobulin M - chemistry</topic><topic>Immunoglobulin Variable Region - blood</topic><topic>Immunoglobulin Variable Region - chemistry</topic><topic>Immunology</topic><topic>Infectious diseases</topic><topic>Medical sciences</topic><topic>Peptide Fragments - immunology</topic><topic>Peptides</topic><topic>Viral diseases</topic><topic>Viral diseases of the lymphoid tissue and the blood. Aids</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>METLAS, R</creatorcontrib><creatorcontrib>TRAJKOVIC, D</creatorcontrib><creatorcontrib>SRDIC, T</creatorcontrib><creatorcontrib>VELJKOVIC, V</creatorcontrib><creatorcontrib>COLOMBATTI, A</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Health and Safety Science Abstracts (Full archive)</collection><collection>Immunology Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Toxicology Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of acquired immune deficiency syndromes (1999)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>METLAS, R</au><au>TRAJKOVIC, D</au><au>SRDIC, T</au><au>VELJKOVIC, V</au><au>COLOMBATTI, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Anti-V3 and anti-IgG antibodies of healthy individuals share complementarity structures</atitle><jtitle>Journal of acquired immune deficiency syndromes (1999)</jtitle><addtitle>J Acquir Immune Defic Syndr</addtitle><date>1999-08-01</date><risdate>1999</risdate><volume>21</volume><issue>4</issue><spage>266</spage><epage>270</epage><pages>266-270</pages><issn>1077-9450</issn><issn>1525-4135</issn><eissn>2331-6993</eissn><eissn>1944-7884</eissn><coden>JDSRET</coden><abstract>It was recently shown that antibodies reactive with a peptide from the tip of the HIV-1NY5 gp120 V3 loop (V3 peptide) are present not only in sera of HIV-positive patients but also in sera of healthy HIV-negative individuals. In the present study, we show that V3 peptide reactive antibodies are predominantly IgM in sera of HIV negative individuals and that a fraction of the IgG anti-V3 antibodies exhibit features of autoantibodies. These antibodies were purified by chromatography on IgG-sepharose columns from sera as well as from purified IgG anti-V3 antibodies. A higher IgG anti-V3 reactivity was detected in autoantibody preparations from HIV-positive sera as compared with the reactivity of sera and purified antibodies from HIV-negative individuals. This was confirmed by solid phase binding of IgG anti-V3 antibodies both to V3 and to human IgG F(ab')2 antigens. The autoantibodies did not bind to peptides that share sequence similarity with V3 peptide indicating a high epitope specificity. The detection of antibodies against HIV epitopes in HIV-negative individuals may suggest that anti-V3 antibodies after HIV infection represent at least in part a secondary immune response.</abstract><cop>New York, NY</cop><pub>Raven Press</pub><pmid>10428103</pmid><doi>10.1097/00126334-199908010-00002</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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subjects | AIDS/HIV Analysis of the immune response. Humoral and cellular immunity Antibodies, Anti-Idiotypic - blood Antibodies, Anti-Idiotypic - chemistry Antibody Affinity Autoantibodies - blood Autoantibodies - chemistry Biological and medical sciences Cell interactions Cross Reactions Fundamental and applied biological sciences. Psychology Fundamental immunology HIV HIV Antibodies - blood HIV Antibodies - chemistry HIV Envelope Protein gp120 - immunology HIV Seronegativity - immunology HIV Seropositivity - immunology Human immunodeficiency virus Human viral diseases Humans Immunobiology Immunoglobulin G - blood Immunoglobulin G - chemistry Immunoglobulin G - immunology Immunoglobulin M - blood Immunoglobulin M - chemistry Immunoglobulin Variable Region - blood Immunoglobulin Variable Region - chemistry Immunology Infectious diseases Medical sciences Peptide Fragments - immunology Peptides Viral diseases Viral diseases of the lymphoid tissue and the blood. Aids |
title | Anti-V3 and anti-IgG antibodies of healthy individuals share complementarity structures |
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