Humanization of chicken monoclonal antibody using phage-display system
We describe a simple method for humanizing chicken monoclonal antibody (mAb). Humanization of mAbs by simple CDR-grafting often results in loss of affinity because certain framework residues of the antibody variable regions can participate in antigen–antibody interaction. In this study, humanization...
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| Veröffentlicht in: | Molecular immunology 2006-02, Vol.43 (6), p.634-642 |
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| container_title | Molecular immunology |
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| creator | Nishibori, Nahoko Horiuchi, Hiroyuki Furusawa, Shuichi Matsuda, Haruo |
| description | We describe a simple method for humanizing chicken monoclonal antibody (mAb). Humanization of mAbs by simple CDR-grafting often results in loss of affinity because certain framework residues of the antibody variable regions can participate in antigen–antibody interaction. In this study, humanization of chicken mAbs was achieved by CDR-grafting, followed by framework fine-tuning using a chicken phage-displayed mAb, phAb4-31, as a model antibody. In order to fine-tune the framework, we used the phage-displayed combinatorial library with permutation of important framework residues. After panning the humanized library, the “most humanized” variants were selected and analyzed for antigen-binding activity. All of these clones retained affinity comparable to the parental chicken mAb. These results suggest that chicken mAbs can easily be humanized, and thus humanized chicken mAbs may be practically applied as therapeutic agents. |
| doi_str_mv | 10.1016/j.molimm.2005.04.002 |
| format | Article |
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Humanization of mAbs by simple CDR-grafting often results in loss of affinity because certain framework residues of the antibody variable regions can participate in antigen–antibody interaction. In this study, humanization of chicken mAbs was achieved by CDR-grafting, followed by framework fine-tuning using a chicken phage-displayed mAb, phAb4-31, as a model antibody. In order to fine-tune the framework, we used the phage-displayed combinatorial library with permutation of important framework residues. After panning the humanized library, the “most humanized” variants were selected and analyzed for antigen-binding activity. All of these clones retained affinity comparable to the parental chicken mAb. These results suggest that chicken mAbs can easily be humanized, and thus humanized chicken mAbs may be practically applied as therapeutic agents.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibody Affinity</subject><subject>Chicken</subject><subject>Chickens</subject><subject>Cloning, Molecular</subject><subject>Complementarity Determining Regions - genetics</subject><subject>Humanization</subject><subject>Humanized antibody</subject><subject>Humans</subject><subject>Immunoglobulin Fab Fragments</subject><subject>Immunoglobulin Variable Region</subject><subject>Methods</subject><subject>Peptide Library</subject><subject>Protein Engineering</subject><issn>0161-5890</issn><issn>1872-9142</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kMFKAzEURYMoWqt_IDIrdzO-ZJJMuxGkWCsU3Og6ZJLXmjpJ6mRGqF_vlBbcuXqbc-_lHUJuKBQUqLzfFD42zvuCAYgCeAHATsiITiqWTylnp2Q0YDQXkylckMuUNgAgQYpzckFlKQEoG5H5ovc6uB_duRiyuMrMhzOfGDIfQzRNDLrJdOhcHe0u65ML62z7odeYW5e2jd5laZc69FfkbKWbhNfHOybv86e32SJfvj6_zB6XueFMdrkwiNRwYUs-EStgmpVYCSt5KWRVa1pVXE4nhlVW2toyVuOU2lJLWtMKa8ByTO4Ovds2fvWYOuVdMtg0OmDsk5KVGCpYOYD8AJo2ptTiSm1b53W7UxTU3p_aqIM_tfengKvB3xC7Pfb3tUf7FzoKG4CHA4DDl98OW5WMw2DQuhZNp2x0_y_8AhKTg7c</recordid><startdate>20060201</startdate><enddate>20060201</enddate><creator>Nishibori, Nahoko</creator><creator>Horiuchi, Hiroyuki</creator><creator>Furusawa, Shuichi</creator><creator>Matsuda, Haruo</creator><general>Elsevier Ltd</general><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>7X8</scope></search><sort><creationdate>20060201</creationdate><title>Humanization of chicken monoclonal antibody using phage-display system</title><author>Nishibori, Nahoko ; Horiuchi, Hiroyuki ; Furusawa, Shuichi ; Matsuda, Haruo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c426t-5cee1c45d3485f02a23e75d643567ba1774698c27d6dbd22be91d3a61b17eb0e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibody Affinity</topic><topic>Chicken</topic><topic>Chickens</topic><topic>Cloning, Molecular</topic><topic>Complementarity Determining Regions - genetics</topic><topic>Humanization</topic><topic>Humanized antibody</topic><topic>Humans</topic><topic>Immunoglobulin Fab Fragments</topic><topic>Immunoglobulin Variable Region</topic><topic>Methods</topic><topic>Peptide Library</topic><topic>Protein Engineering</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nishibori, Nahoko</creatorcontrib><creatorcontrib>Horiuchi, Hiroyuki</creatorcontrib><creatorcontrib>Furusawa, Shuichi</creatorcontrib><creatorcontrib>Matsuda, Haruo</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Molecular immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nishibori, Nahoko</au><au>Horiuchi, Hiroyuki</au><au>Furusawa, Shuichi</au><au>Matsuda, Haruo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Humanization of chicken monoclonal antibody using phage-display system</atitle><jtitle>Molecular immunology</jtitle><addtitle>Mol Immunol</addtitle><date>2006-02-01</date><risdate>2006</risdate><volume>43</volume><issue>6</issue><spage>634</spage><epage>642</epage><pages>634-642</pages><issn>0161-5890</issn><eissn>1872-9142</eissn><abstract>We describe a simple method for humanizing chicken monoclonal antibody (mAb). Humanization of mAbs by simple CDR-grafting often results in loss of affinity because certain framework residues of the antibody variable regions can participate in antigen–antibody interaction. In this study, humanization of chicken mAbs was achieved by CDR-grafting, followed by framework fine-tuning using a chicken phage-displayed mAb, phAb4-31, as a model antibody. In order to fine-tune the framework, we used the phage-displayed combinatorial library with permutation of important framework residues. After panning the humanized library, the “most humanized” variants were selected and analyzed for antigen-binding activity. All of these clones retained affinity comparable to the parental chicken mAb. 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| ispartof | Molecular immunology, 2006-02, Vol.43 (6), p.634-642 |
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| language | eng |
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| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | Animals Antibodies, Monoclonal - genetics Antibody Affinity Chicken Chickens Cloning, Molecular Complementarity Determining Regions - genetics Humanization Humanized antibody Humans Immunoglobulin Fab Fragments Immunoglobulin Variable Region Methods Peptide Library Protein Engineering |
| title | Humanization of chicken monoclonal antibody using phage-display system |
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