Humanization and characterization of the anti‐HLA‐DR antibody 1D10
1D10 is a previously described antibody that binds to cells from a majority of B‐cell malignancies. The current studies were designed to further evaluate the antigen specificity of 1D10 and its potential as an immunotherapeutic agent. Studies with transfectants and immunoprecipitation demonstrated t...
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Veröffentlicht in: | International journal of cancer 2001-08, Vol.93 (4), p.556-565 |
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container_title | International journal of cancer |
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creator | Kostelny, Sheri A. Link, Brian K. Tso, J. Yun Vasquez, Max Jorgensen, Brett H. Wang, Hong Hall, William C. Weiner, George J. |
description | 1D10 is a previously described antibody that binds to cells from a majority of B‐cell malignancies. The current studies were designed to further evaluate the antigen specificity of 1D10 and its potential as an immunotherapeutic agent. Studies with transfectants and immunoprecipitation demonstrated that 1D10 recognizes some, but not all, of the human HLA‐DR β chains. Both normal and malignant B cells can express the 1D10 antigen. A humanized version of 1D10 was produced using CDR grafting. The resulting antibody has an affinity that is similar to that of the parental murine antibody. In addition, the humanized antibody is capable of inducing complement‐mediated cytotoxicity, antibody‐dependent cell cytotoxicity, and direct apoptosis of 1D10‐expressing B cells. Based on these in vitro anti‐tumor activities, we conclude humanized 1D10 deserves further evaluation as an immunotherapeutic agent. © 2001 Wiley‐Liss, Inc. |
doi_str_mv | 10.1002/ijc.1366 |
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Yun ; Vasquez, Max ; Jorgensen, Brett H. ; Wang, Hong ; Hall, William C. ; Weiner, George J.</creator><creatorcontrib>Kostelny, Sheri A. ; Link, Brian K. ; Tso, J. Yun ; Vasquez, Max ; Jorgensen, Brett H. ; Wang, Hong ; Hall, William C. ; Weiner, George J.</creatorcontrib><description>1D10 is a previously described antibody that binds to cells from a majority of B‐cell malignancies. The current studies were designed to further evaluate the antigen specificity of 1D10 and its potential as an immunotherapeutic agent. Studies with transfectants and immunoprecipitation demonstrated that 1D10 recognizes some, but not all, of the human HLA‐DR β chains. Both normal and malignant B cells can express the 1D10 antigen. A humanized version of 1D10 was produced using CDR grafting. The resulting antibody has an affinity that is similar to that of the parental murine antibody. In addition, the humanized antibody is capable of inducing complement‐mediated cytotoxicity, antibody‐dependent cell cytotoxicity, and direct apoptosis of 1D10‐expressing B cells. Based on these in vitro anti‐tumor activities, we conclude humanized 1D10 deserves further evaluation as an immunotherapeutic agent. © 2001 Wiley‐Liss, Inc.</description><identifier>ISSN: 0020-7136</identifier><identifier>EISSN: 1097-0215</identifier><identifier>DOI: 10.1002/ijc.1366</identifier><identifier>PMID: 11477560</identifier><identifier>CODEN: IJCNAW</identifier><language>eng</language><publisher>New York: John Wiley & Sons, Inc</publisher><subject>Amino Acid Sequence ; Animals ; Antibodies, Monoclonal - biosynthesis ; Antibodies, Monoclonal - genetics ; Antibodies, Monoclonal - immunology ; Antibody Affinity ; Antibody Specificity ; Antibody-Dependent Cell Cytotoxicity ; Antineoplastic agents ; Apoptosis - immunology ; Biological and medical sciences ; Cloning, Molecular ; Epitopes - immunology ; histocompatibility antigen HLA ; HLA-DR Antigens - immunology ; HLA‐DR ; Humans ; Immunoglobulin G - biosynthesis ; Immunoglobulin G - genetics ; Immunoglobulin G - immunology ; Immunotherapy ; Leukemia, T-Cell - immunology ; Leukemia, T-Cell - pathology ; lymphoma ; Lymphoma, B-Cell - immunology ; Lymphoma, B-Cell - pathology ; Medical sciences ; MHC class II ; Mice ; Molecular Sequence Data ; monoclonal antibody ; Pharmacology. Drug treatments ; Sequence Homology, Amino Acid ; Tumor Cells, Cultured</subject><ispartof>International journal of cancer, 2001-08, Vol.93 (4), p.556-565</ispartof><rights>Copyright © 2001 Wiley‐Liss, Inc.</rights><rights>2002 INIST-CNRS</rights><rights>Copyright 2001 Wiley-Liss, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4126-407dd91b0afc1ddd6832fbce720792d3500f585da6e2aca1b5121705c27689ae3</citedby><cites>FETCH-LOGICAL-c4126-407dd91b0afc1ddd6832fbce720792d3500f585da6e2aca1b5121705c27689ae3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fijc.1366$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fijc.1366$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=14093459$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11477560$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kostelny, Sheri A.</creatorcontrib><creatorcontrib>Link, Brian K.</creatorcontrib><creatorcontrib>Tso, J. Yun</creatorcontrib><creatorcontrib>Vasquez, Max</creatorcontrib><creatorcontrib>Jorgensen, Brett H.</creatorcontrib><creatorcontrib>Wang, Hong</creatorcontrib><creatorcontrib>Hall, William C.</creatorcontrib><creatorcontrib>Weiner, George J.</creatorcontrib><title>Humanization and characterization of the anti‐HLA‐DR antibody 1D10</title><title>International journal of cancer</title><addtitle>Int J Cancer</addtitle><description>1D10 is a previously described antibody that binds to cells from a majority of B‐cell malignancies. The current studies were designed to further evaluate the antigen specificity of 1D10 and its potential as an immunotherapeutic agent. Studies with transfectants and immunoprecipitation demonstrated that 1D10 recognizes some, but not all, of the human HLA‐DR β chains. Both normal and malignant B cells can express the 1D10 antigen. A humanized version of 1D10 was produced using CDR grafting. The resulting antibody has an affinity that is similar to that of the parental murine antibody. In addition, the humanized antibody is capable of inducing complement‐mediated cytotoxicity, antibody‐dependent cell cytotoxicity, and direct apoptosis of 1D10‐expressing B cells. Based on these in vitro anti‐tumor activities, we conclude humanized 1D10 deserves further evaluation as an immunotherapeutic agent. © 2001 Wiley‐Liss, Inc.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - biosynthesis</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibody Affinity</subject><subject>Antibody Specificity</subject><subject>Antibody-Dependent Cell Cytotoxicity</subject><subject>Antineoplastic agents</subject><subject>Apoptosis - immunology</subject><subject>Biological and medical sciences</subject><subject>Cloning, Molecular</subject><subject>Epitopes - immunology</subject><subject>histocompatibility antigen HLA</subject><subject>HLA-DR Antigens - immunology</subject><subject>HLA‐DR</subject><subject>Humans</subject><subject>Immunoglobulin G - biosynthesis</subject><subject>Immunoglobulin G - genetics</subject><subject>Immunoglobulin G - immunology</subject><subject>Immunotherapy</subject><subject>Leukemia, T-Cell - immunology</subject><subject>Leukemia, T-Cell - pathology</subject><subject>lymphoma</subject><subject>Lymphoma, B-Cell - immunology</subject><subject>Lymphoma, B-Cell - pathology</subject><subject>Medical sciences</subject><subject>MHC class II</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>monoclonal antibody</subject><subject>Pharmacology. Drug treatments</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tumor Cells, Cultured</subject><issn>0020-7136</issn><issn>1097-0215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqF0N1KwzAUB_AgiptT8AmkN4o3neekTdNejs25yUAQvS5pkrKOfsymReaVj-Az-iRmW2VXYi4STs6Pc-BPyCXCEAHoXbaSQ_SC4Ij0ESLuAkV2TPq2BS63jR45M2YFgMjAPyU9RJ9zFkCfTGdtIcrsQzRZVTqiVI5cilrIRte_n1XqNEtte032_fk1W4zsPXne1UmlNg5OEM7JSSpyoy-6d0Bep_cv45m7eHqYj0cLV_pIA9cHrlSECYhUolIqCD2aJlJzCjyiymMAKQuZEoGmQgpMGFLkwCTlQRgJ7Q3IzX7uuq7eWm2auMiM1HkuSl21JuYIfujZ8x_EEDmPOLfwdg9lXRlT6zRe11kh6k2MEG_DjW248TZcS6-6mW1SaHWAXZoWXHdAGCnytBalzMzB-RB5Pousc_fuPcv15s-F8fxxvFv8A_utj3k</recordid><startdate>20010815</startdate><enddate>20010815</enddate><creator>Kostelny, Sheri A.</creator><creator>Link, Brian K.</creator><creator>Tso, J. Yun</creator><creator>Vasquez, Max</creator><creator>Jorgensen, Brett H.</creator><creator>Wang, Hong</creator><creator>Hall, William C.</creator><creator>Weiner, George J.</creator><general>John Wiley & Sons, Inc</general><general>Wiley-Liss</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>8FD</scope><scope>FR3</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20010815</creationdate><title>Humanization and characterization of the anti‐HLA‐DR antibody 1D10</title><author>Kostelny, Sheri A. ; Link, Brian K. ; Tso, J. Yun ; Vasquez, Max ; Jorgensen, Brett H. ; Wang, Hong ; Hall, William C. ; Weiner, George J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4126-407dd91b0afc1ddd6832fbce720792d3500f585da6e2aca1b5121705c27689ae3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - biosynthesis</topic><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibody Affinity</topic><topic>Antibody Specificity</topic><topic>Antibody-Dependent Cell Cytotoxicity</topic><topic>Antineoplastic agents</topic><topic>Apoptosis - immunology</topic><topic>Biological and medical sciences</topic><topic>Cloning, Molecular</topic><topic>Epitopes - immunology</topic><topic>histocompatibility antigen HLA</topic><topic>HLA-DR Antigens - immunology</topic><topic>HLA‐DR</topic><topic>Humans</topic><topic>Immunoglobulin G - biosynthesis</topic><topic>Immunoglobulin G - genetics</topic><topic>Immunoglobulin G - immunology</topic><topic>Immunotherapy</topic><topic>Leukemia, T-Cell - immunology</topic><topic>Leukemia, T-Cell - pathology</topic><topic>lymphoma</topic><topic>Lymphoma, B-Cell - immunology</topic><topic>Lymphoma, B-Cell - pathology</topic><topic>Medical sciences</topic><topic>MHC class II</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>monoclonal antibody</topic><topic>Pharmacology. Drug treatments</topic><topic>Sequence Homology, Amino Acid</topic><topic>Tumor Cells, Cultured</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kostelny, Sheri A.</creatorcontrib><creatorcontrib>Link, Brian K.</creatorcontrib><creatorcontrib>Tso, J. Yun</creatorcontrib><creatorcontrib>Vasquez, Max</creatorcontrib><creatorcontrib>Jorgensen, Brett H.</creatorcontrib><creatorcontrib>Wang, Hong</creatorcontrib><creatorcontrib>Hall, William C.</creatorcontrib><creatorcontrib>Weiner, George J.</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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>International journal of cancer</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kostelny, Sheri A.</au><au>Link, Brian K.</au><au>Tso, J. Yun</au><au>Vasquez, Max</au><au>Jorgensen, Brett H.</au><au>Wang, Hong</au><au>Hall, William C.</au><au>Weiner, George J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Humanization and characterization of the anti‐HLA‐DR antibody 1D10</atitle><jtitle>International journal of cancer</jtitle><addtitle>Int J Cancer</addtitle><date>2001-08-15</date><risdate>2001</risdate><volume>93</volume><issue>4</issue><spage>556</spage><epage>565</epage><pages>556-565</pages><issn>0020-7136</issn><eissn>1097-0215</eissn><coden>IJCNAW</coden><abstract>1D10 is a previously described antibody that binds to cells from a majority of B‐cell malignancies. The current studies were designed to further evaluate the antigen specificity of 1D10 and its potential as an immunotherapeutic agent. Studies with transfectants and immunoprecipitation demonstrated that 1D10 recognizes some, but not all, of the human HLA‐DR β chains. Both normal and malignant B cells can express the 1D10 antigen. A humanized version of 1D10 was produced using CDR grafting. The resulting antibody has an affinity that is similar to that of the parental murine antibody. In addition, the humanized antibody is capable of inducing complement‐mediated cytotoxicity, antibody‐dependent cell cytotoxicity, and direct apoptosis of 1D10‐expressing B cells. Based on these in vitro anti‐tumor activities, we conclude humanized 1D10 deserves further evaluation as an immunotherapeutic agent. © 2001 Wiley‐Liss, Inc.</abstract><cop>New York</cop><pub>John Wiley & Sons, Inc</pub><pmid>11477560</pmid><doi>10.1002/ijc.1366</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Antibodies, Monoclonal - biosynthesis Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibody Affinity Antibody Specificity Antibody-Dependent Cell Cytotoxicity Antineoplastic agents Apoptosis - immunology Biological and medical sciences Cloning, Molecular Epitopes - immunology histocompatibility antigen HLA HLA-DR Antigens - immunology HLA‐DR Humans Immunoglobulin G - biosynthesis Immunoglobulin G - genetics Immunoglobulin G - immunology Immunotherapy Leukemia, T-Cell - immunology Leukemia, T-Cell - pathology lymphoma Lymphoma, B-Cell - immunology Lymphoma, B-Cell - pathology Medical sciences MHC class II Mice Molecular Sequence Data monoclonal antibody Pharmacology. Drug treatments Sequence Homology, Amino Acid Tumor Cells, Cultured |
title | Humanization and characterization of the anti‐HLA‐DR antibody 1D10 |
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