A technology platform for the fast production of monoclonal recombinant antibodies against plant proteins and peptides
The application of recombinant antibodies in plant biology research is limited because plant researchers have minimal access to high-quality phage display libraries. Therefore, we constructed a library of 1.3×10 10 clones displaying human single-chain variable fragments (scFvs) that is available to...
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Veröffentlicht in: | Journal of immunological methods 2004-11, Vol.294 (1), p.181-187 |
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container_title | Journal of immunological methods |
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creator | Eeckhout, Dominique De Clercq, Annelies Van De Slijke, Eveline Van Leene, Jelle Stals, Hilde Casteels, Peter Persiau, Geert Vercammen, Dominique Van Breusegem, Frank Zabeau, Marc Inzé, Dirk Jespers, Laurent Depicker, Ann De Jaeger, Geert |
description | The application of recombinant antibodies in plant biology research is limited because plant researchers have minimal access to high-quality phage display libraries. Therefore, we constructed a library of 1.3×10
10 clones displaying human single-chain variable fragments (scFvs) that is available to the academic community. The scFvs selected from the library against a diverse set of plant proteins showed moderate to high antigen-binding affinity together with high specificity. Moreover, to optimize an scFv as immunodetection agent, two expression systems that allow efficient production and purification of bivalent scFv–Fc and scFv–C
κZIP fusion proteins were integrated. We are convinced that this antibody platform will further stimulate applications of recombinant antibodies such as the diagnostic detection or immunomodulation of specific antigens in plants. |
doi_str_mv | 10.1016/j.jim.2004.08.006 |
format | Article |
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10 clones displaying human single-chain variable fragments (scFvs) that is available to the academic community. The scFvs selected from the library against a diverse set of plant proteins showed moderate to high antigen-binding affinity together with high specificity. Moreover, to optimize an scFv as immunodetection agent, two expression systems that allow efficient production and purification of bivalent scFv–Fc and scFv–C
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10 clones displaying human single-chain variable fragments (scFvs) that is available to the academic community. The scFvs selected from the library against a diverse set of plant proteins showed moderate to high antigen-binding affinity together with high specificity. Moreover, to optimize an scFv as immunodetection agent, two expression systems that allow efficient production and purification of bivalent scFv–Fc and scFv–C
κZIP fusion proteins were integrated. We are convinced that this antibody platform will further stimulate applications of recombinant antibodies such as the diagnostic detection or immunomodulation of specific antigens in plants.</description><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibody Affinity - genetics</subject><subject>Antibody Affinity - immunology</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - genetics</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fundamental immunology</subject><subject>Gene Expression</subject><subject>Gene Library</subject><subject>Humans</subject><subject>Immunoglobulin kappa-Chains - genetics</subject><subject>Immunoglobulin Variable Region - genetics</subject><subject>Immunoglobulin Variable Region - immunology</subject><subject>Immunoglobulin Variable Region - isolation & purification</subject><subject>Molecular immunology</subject><subject>Peptides - immunology</subject><subject>Phage display</subject><subject>Plant</subject><subject>Plant Proteins - immunology</subject><subject>Recombinant antibody</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Single-chain variable fragment</subject><subject>Substrate Specificity - genetics</subject><subject>Substrate Specificity - immunology</subject><subject>Techniques</subject><issn>0022-1759</issn><issn>1872-7905</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2004</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUFr3DAUhEVpaLbb_oBeii7Nzc6TZEk2PYXQtIVAL-1ZyNJzosW2XEsbyL-vzC7k1ggkIfTNY5gh5BODmgFT14f6EKaaAzQ1tDWAekN2rNW80h3It2QHwHnFtOwuyfuUDgDAQME7csmkgga42pGnG5rRPc5xjA_PdBltHuI60XLQ_Ih0sCnTZY3-6HKIM40DneIc3RhnO9IVXZz6MNs507JDH33ARO2DDfOmG7ePos5Y3oXwdMElB4_pA7kY7Jjw4_nekz93337f_qjuf33_eXtzX7mmEbnqfCdBd3xQ3CFjgmvRCeGca3wPQ2uZ6p3A1gtQDp2U1rZMMumxZ9ppLcWeXJ3mFhd_j5iymUJyOBZnGI_JKM20Elq8CnLQZYF-FSxxC6n5BrIT6NaY0oqDWdYw2fXZMDBbfeZgSn1mq89Aa0p9RfP5PPzYT-hfFOe-CvDlDNjk7DisdnYhvXBKCNWUjPbk64nDEu5TwNUkF3B26EMpLRsfw39s_AONjbl8</recordid><startdate>20041101</startdate><enddate>20041101</enddate><creator>Eeckhout, Dominique</creator><creator>De Clercq, Annelies</creator><creator>Van De Slijke, Eveline</creator><creator>Van Leene, Jelle</creator><creator>Stals, Hilde</creator><creator>Casteels, Peter</creator><creator>Persiau, Geert</creator><creator>Vercammen, Dominique</creator><creator>Van Breusegem, Frank</creator><creator>Zabeau, Marc</creator><creator>Inzé, Dirk</creator><creator>Jespers, Laurent</creator><creator>Depicker, Ann</creator><creator>De Jaeger, Geert</creator><general>Elsevier B.V</general><general>Elsevier</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>7QO</scope><scope>7T5</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20041101</creationdate><title>A technology platform for the fast production of monoclonal recombinant antibodies against plant proteins and peptides</title><author>Eeckhout, Dominique ; De Clercq, Annelies ; Van De Slijke, Eveline ; Van Leene, Jelle ; Stals, Hilde ; Casteels, Peter ; Persiau, Geert ; Vercammen, Dominique ; Van Breusegem, Frank ; Zabeau, Marc ; Inzé, Dirk ; Jespers, Laurent ; Depicker, Ann ; De Jaeger, Geert</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c443t-9d950792f62ce113273933ccc4db0f8a16bc3e8d306cec55aa81515deb17c7753</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2004</creationdate><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibody Affinity - genetics</topic><topic>Antibody Affinity - immunology</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - genetics</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fundamental immunology</topic><topic>Gene Expression</topic><topic>Gene Library</topic><topic>Humans</topic><topic>Immunoglobulin kappa-Chains - genetics</topic><topic>Immunoglobulin Variable Region - genetics</topic><topic>Immunoglobulin Variable Region - immunology</topic><topic>Immunoglobulin Variable Region - isolation & purification</topic><topic>Molecular immunology</topic><topic>Peptides - immunology</topic><topic>Phage display</topic><topic>Plant</topic><topic>Plant Proteins - immunology</topic><topic>Recombinant antibody</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Single-chain variable fragment</topic><topic>Substrate Specificity - genetics</topic><topic>Substrate Specificity - immunology</topic><topic>Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Eeckhout, Dominique</creatorcontrib><creatorcontrib>De Clercq, Annelies</creatorcontrib><creatorcontrib>Van De Slijke, Eveline</creatorcontrib><creatorcontrib>Van Leene, Jelle</creatorcontrib><creatorcontrib>Stals, Hilde</creatorcontrib><creatorcontrib>Casteels, Peter</creatorcontrib><creatorcontrib>Persiau, Geert</creatorcontrib><creatorcontrib>Vercammen, Dominique</creatorcontrib><creatorcontrib>Van Breusegem, Frank</creatorcontrib><creatorcontrib>Zabeau, Marc</creatorcontrib><creatorcontrib>Inzé, Dirk</creatorcontrib><creatorcontrib>Jespers, Laurent</creatorcontrib><creatorcontrib>Depicker, Ann</creatorcontrib><creatorcontrib>De Jaeger, Geert</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>Biotechnology Research Abstracts</collection><collection>Immunology Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of immunological methods</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Eeckhout, Dominique</au><au>De Clercq, Annelies</au><au>Van De Slijke, Eveline</au><au>Van Leene, Jelle</au><au>Stals, Hilde</au><au>Casteels, Peter</au><au>Persiau, Geert</au><au>Vercammen, Dominique</au><au>Van Breusegem, Frank</au><au>Zabeau, Marc</au><au>Inzé, Dirk</au><au>Jespers, Laurent</au><au>Depicker, Ann</au><au>De Jaeger, Geert</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A technology platform for the fast production of monoclonal recombinant antibodies against plant proteins and peptides</atitle><jtitle>Journal of immunological methods</jtitle><addtitle>J Immunol Methods</addtitle><date>2004-11-01</date><risdate>2004</risdate><volume>294</volume><issue>1</issue><spage>181</spage><epage>187</epage><pages>181-187</pages><issn>0022-1759</issn><eissn>1872-7905</eissn><coden>JIMMBG</coden><abstract>The application of recombinant antibodies in plant biology research is limited because plant researchers have minimal access to high-quality phage display libraries. Therefore, we constructed a library of 1.3×10
10 clones displaying human single-chain variable fragments (scFvs) that is available to the academic community. The scFvs selected from the library against a diverse set of plant proteins showed moderate to high antigen-binding affinity together with high specificity. Moreover, to optimize an scFv as immunodetection agent, two expression systems that allow efficient production and purification of bivalent scFv–Fc and scFv–C
κZIP fusion proteins were integrated. We are convinced that this antibody platform will further stimulate applications of recombinant antibodies such as the diagnostic detection or immunomodulation of specific antigens in plants.</abstract><cop>Amsterdam</cop><pub>Elsevier B.V</pub><pmid>15604026</pmid><doi>10.1016/j.jim.2004.08.006</doi><tpages>7</tpages></addata></record> |
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subjects | Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibody Affinity - genetics Antibody Affinity - immunology Biological and medical sciences Carrier Proteins - genetics Fundamental and applied biological sciences. Psychology Fundamental immunology Gene Expression Gene Library Humans Immunoglobulin kappa-Chains - genetics Immunoglobulin Variable Region - genetics Immunoglobulin Variable Region - immunology Immunoglobulin Variable Region - isolation & purification Molecular immunology Peptides - immunology Phage display Plant Plant Proteins - immunology Recombinant antibody Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - immunology Recombinant Fusion Proteins - isolation & purification Single-chain variable fragment Substrate Specificity - genetics Substrate Specificity - immunology Techniques |
title | A technology platform for the fast production of monoclonal recombinant antibodies against plant proteins and peptides |
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