Construction and characterization of a new chimeric antibody against HER2
Immunotherapy with anti-HER2 antibodies has shown promising results in patients with HER2-positive breast cancer. We have recently reported characterization of a mouse monoclonal antibody (mAb) against HER2, which binds to an epitope different from that recognized by trastuzumab and specifically inh...
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| Veröffentlicht in: | IMMUNOTHERAPY 2013-07, Vol.5 (7), p.703-715 |
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| creator | Amiri, Mohammad Mehdi Jeddi-Tehrani, Mahmood Kazemi, Tohid Bahadori, Motahareh Maddah, Mahshid Hojjat-Farsangi, Mohammad Khoshnoodi, Jalal Rabbani, Hodjatallah Shokri, Fazel |
| description | Immunotherapy with anti-HER2 antibodies has shown promising results in patients with HER2-positive breast cancer. We have recently reported characterization of a mouse monoclonal antibody (mAb) against HER2, which binds to an epitope different from that recognized by trastuzumab and specifically inhibits proliferation of tumor cells overexpressing HER2. In the present study we report chimerization of this antibody.
The immunoglobulin variable region heavy and light chain genes of 1T0 hybridoma cells were amplified and ligated to human -1 and constant region genes using splice overlap extension PCR. The chimeric antibody was subsequently expressed and characterized by ELISA, western blot and flow cytometry.
The purified chimeric antibody specifically binds to recombinant HER2 and HER2-overexpressing tumor cells and inhibits proliferation of these cells. The binding affinity of the chimeric mAb was comparable with the parental mouse mAb.
This chimeric anti-HER2 mAb is a potentially valuable tool for targeted immunotherapy. |
| doi_str_mv | 10.2217/imt.13.67 |
| format | Article |
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The immunoglobulin variable region heavy and light chain genes of 1T0 hybridoma cells were amplified and ligated to human -1 and constant region genes using splice overlap extension PCR. The chimeric antibody was subsequently expressed and characterized by ELISA, western blot and flow cytometry.
The purified chimeric antibody specifically binds to recombinant HER2 and HER2-overexpressing tumor cells and inhibits proliferation of these cells. The binding affinity of the chimeric mAb was comparable with the parental mouse mAb.
This chimeric anti-HER2 mAb is a potentially valuable tool for targeted immunotherapy.</description><identifier>ISSN: 1750-743X</identifier><identifier>ISSN: 1750-7448</identifier><identifier>EISSN: 1750-7448</identifier><identifier>DOI: 10.2217/imt.13.67</identifier><identifier>PMID: 23829622</identifier><language>eng</language><publisher>England: Future Medicine Ltd</publisher><subject>Animals ; Antibodies, Monoclonal - genetics ; Antibodies, Monoclonal - immunology ; Antibodies, Monoclonal - therapeutic use ; Binding sites ; Biological activity ; Breast cancer ; Breast Neoplasms - immunology ; Breast Neoplasms - therapy ; Cancer och onkologi ; Care and treatment ; Cell Proliferation ; Chemical properties ; chimeric antibody ; Deoxyribonucleic acid ; DNA ; Enzyme-linked immunosorbent assay ; Female ; Genetic aspects ; Health aspects ; HER2 ; Humans ; Hybridomas ; Immunization, Passive - methods ; Immunodominant Epitopes - immunology ; Immunologi inom det medicinska området ; Kinases ; Klinisk medicin ; MEDICAL AND HEALTH SCIENCES ; MEDICIN OCH HÄLSOVETENSKAP ; Medicinska och farmaceutiska grundvetenskaper ; Mice ; Molecular Targeted Therapy ; Molecular weight ; Monoclonal antibodies ; monoclonal antibody ; Protein Engineering - methods ; Proteins ; Receptor, ErbB-2 - antagonists & inhibitors ; Receptor, ErbB-2 - immunology ; Recombinant Fusion Proteins - genetics ; Recombinant Fusion Proteins - immunology ; Recombinant Fusion Proteins - therapeutic use</subject><ispartof>IMMUNOTHERAPY, 2013-07, Vol.5 (7), p.703-715</ispartof><rights>COPYRIGHT 2013 Future Medicine Ltd.</rights><rights>2013 Future Medicine Ltd</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c696t-28e907a7a84514f02981b17cb925e2f053fa35cb4af4dbd67c19501b9c2df9b3</citedby><cites>FETCH-LOGICAL-c696t-28e907a7a84514f02981b17cb925e2f053fa35cb4af4dbd67c19501b9c2df9b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,552,780,885</link.rule.ids><linktorsrc>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:127279940$$EView_record_in_Swedish_Publication_Index_(SWEPUB)$$FView_record_in_$$GSwedish_Publication_Index_(SWEPUB)$$Hfree_for_read</linktorsrc><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/23829622$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttp://hdl.handle.net/10616/41753$$DView record from Swedish Publication Index$$Hfree_for_read</backlink><backlink>$$Uhttp://kipublications.ki.se/Default.aspx?queryparsed=id:127279940$$DView record from Swedish Publication Index$$Hfree_for_read</backlink></links><search><creatorcontrib>Amiri, Mohammad Mehdi</creatorcontrib><creatorcontrib>Jeddi-Tehrani, Mahmood</creatorcontrib><creatorcontrib>Kazemi, Tohid</creatorcontrib><creatorcontrib>Bahadori, Motahareh</creatorcontrib><creatorcontrib>Maddah, Mahshid</creatorcontrib><creatorcontrib>Hojjat-Farsangi, Mohammad</creatorcontrib><creatorcontrib>Khoshnoodi, Jalal</creatorcontrib><creatorcontrib>Rabbani, Hodjatallah</creatorcontrib><creatorcontrib>Shokri, Fazel</creatorcontrib><creatorcontrib>Dept of Oncology-Pathology</creatorcontrib><creatorcontrib>Karolinska Institutet</creatorcontrib><creatorcontrib>Inst för onkologi-patologi</creatorcontrib><title>Construction and characterization of a new chimeric antibody against HER2</title><title>IMMUNOTHERAPY</title><addtitle>Immunotherapy</addtitle><description>Immunotherapy with anti-HER2 antibodies has shown promising results in patients with HER2-positive breast cancer. We have recently reported characterization of a mouse monoclonal antibody (mAb) against HER2, which binds to an epitope different from that recognized by trastuzumab and specifically inhibits proliferation of tumor cells overexpressing HER2. In the present study we report chimerization of this antibody.
The immunoglobulin variable region heavy and light chain genes of 1T0 hybridoma cells were amplified and ligated to human -1 and constant region genes using splice overlap extension PCR. The chimeric antibody was subsequently expressed and characterized by ELISA, western blot and flow cytometry.
The purified chimeric antibody specifically binds to recombinant HER2 and HER2-overexpressing tumor cells and inhibits proliferation of these cells. The binding affinity of the chimeric mAb was comparable with the parental mouse mAb.
This chimeric anti-HER2 mAb is a potentially valuable tool for targeted immunotherapy.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibodies, Monoclonal - therapeutic use</subject><subject>Binding sites</subject><subject>Biological activity</subject><subject>Breast cancer</subject><subject>Breast Neoplasms - immunology</subject><subject>Breast Neoplasms - therapy</subject><subject>Cancer och onkologi</subject><subject>Care and treatment</subject><subject>Cell Proliferation</subject><subject>Chemical properties</subject><subject>chimeric antibody</subject><subject>Deoxyribonucleic acid</subject><subject>DNA</subject><subject>Enzyme-linked immunosorbent assay</subject><subject>Female</subject><subject>Genetic aspects</subject><subject>Health aspects</subject><subject>HER2</subject><subject>Humans</subject><subject>Hybridomas</subject><subject>Immunization, Passive - methods</subject><subject>Immunodominant Epitopes - immunology</subject><subject>Immunologi inom det medicinska området</subject><subject>Kinases</subject><subject>Klinisk medicin</subject><subject>MEDICAL AND HEALTH SCIENCES</subject><subject>MEDICIN OCH HÄLSOVETENSKAP</subject><subject>Medicinska och farmaceutiska grundvetenskaper</subject><subject>Mice</subject><subject>Molecular Targeted Therapy</subject><subject>Molecular weight</subject><subject>Monoclonal antibodies</subject><subject>monoclonal antibody</subject><subject>Protein Engineering - methods</subject><subject>Proteins</subject><subject>Receptor, ErbB-2 - antagonists & inhibitors</subject><subject>Receptor, ErbB-2 - immunology</subject><subject>Recombinant Fusion Proteins - genetics</subject><subject>Recombinant Fusion Proteins - immunology</subject><subject>Recombinant Fusion Proteins - therapeutic use</subject><issn>1750-743X</issn><issn>1750-7448</issn><issn>1750-7448</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2013</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>D8T</sourceid><recordid>eNqNkktv1DAQgCMEoqVw4A-gSFzgsItfseNjtSq0UiUk1AM3y3HGxWVjL3ZCVX49s91H1aqVqhxiT75vYs9MVb2nZM4YVV_CMM4pn0v1ojqkqiEzJUT7cr_mPw-qN6VcESKFkuJ1dcB4y7Rk7LA6W6RYxjy5MaRY29jX7pfN1o2Qwz97G0y-tnWEa_wSBgw7xMbQpf6mtpc2oF6fnvxgb6tX3i4LvNu-j6qLrycXi9PZ-fdvZ4vj85mTWo4z1oImyirbioYKT5huaUeV6zRrgHnScG954zphvei7XipHdUNopx3rve74UTXbpC3XsJo6s8phsPnGJBvMNvQbV2Aa1nJNkddP8quc-jtpJ1KmmNJaEHTVk25aQbQZS_IXdh6RVBqBRedoftqY-Is_E5TRDKE4WC5thDQVQwVThFIm1TNQqrnUrdDPRBnlAtGPD9CrNOWIjTGUY8kZNoHdUZd2CSZEn0bs_TqpOea8aTXhdH2Z-SMUPj0MwaUIPmD8nvB5I7icSsng95WjxKwn1uDE4jnM7fU_bA86dQP0e3I3ogg0G8BP45ShuADRgdns0AguRHgk8X9DU_cr</recordid><startdate>20130701</startdate><enddate>20130701</enddate><creator>Amiri, Mohammad Mehdi</creator><creator>Jeddi-Tehrani, Mahmood</creator><creator>Kazemi, Tohid</creator><creator>Bahadori, Motahareh</creator><creator>Maddah, Mahshid</creator><creator>Hojjat-Farsangi, Mohammad</creator><creator>Khoshnoodi, Jalal</creator><creator>Rabbani, Hodjatallah</creator><creator>Shokri, Fazel</creator><general>Future Medicine 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>3V.</scope><scope>7T5</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>EHMNL</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>ADTPV</scope><scope>AOWAS</scope><scope>D8T</scope><scope>ZZAVC</scope></search><sort><creationdate>20130701</creationdate><title>Construction and characterization of a new chimeric antibody against HER2</title><author>Amiri, Mohammad Mehdi ; Jeddi-Tehrani, Mahmood ; Kazemi, Tohid ; Bahadori, Motahareh ; Maddah, Mahshid ; Hojjat-Farsangi, Mohammad ; Khoshnoodi, Jalal ; Rabbani, Hodjatallah ; Shokri, Fazel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c696t-28e907a7a84514f02981b17cb925e2f053fa35cb4af4dbd67c19501b9c2df9b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2013</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibodies, Monoclonal - therapeutic use</topic><topic>Binding sites</topic><topic>Biological activity</topic><topic>Breast cancer</topic><topic>Breast Neoplasms - immunology</topic><topic>Breast Neoplasms - therapy</topic><topic>Cancer och onkologi</topic><topic>Care and treatment</topic><topic>Cell Proliferation</topic><topic>Chemical properties</topic><topic>chimeric antibody</topic><topic>Deoxyribonucleic acid</topic><topic>DNA</topic><topic>Enzyme-linked immunosorbent assay</topic><topic>Female</topic><topic>Genetic aspects</topic><topic>Health aspects</topic><topic>HER2</topic><topic>Humans</topic><topic>Hybridomas</topic><topic>Immunization, Passive - methods</topic><topic>Immunodominant Epitopes - immunology</topic><topic>Immunologi inom det medicinska området</topic><topic>Kinases</topic><topic>Klinisk medicin</topic><topic>MEDICAL AND HEALTH SCIENCES</topic><topic>MEDICIN OCH HÄLSOVETENSKAP</topic><topic>Medicinska och farmaceutiska grundvetenskaper</topic><topic>Mice</topic><topic>Molecular Targeted Therapy</topic><topic>Molecular weight</topic><topic>Monoclonal antibodies</topic><topic>monoclonal antibody</topic><topic>Protein Engineering - methods</topic><topic>Proteins</topic><topic>Receptor, ErbB-2 - antagonists & inhibitors</topic><topic>Receptor, ErbB-2 - immunology</topic><topic>Recombinant Fusion Proteins - genetics</topic><topic>Recombinant Fusion Proteins - immunology</topic><topic>Recombinant Fusion Proteins - therapeutic use</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Amiri, Mohammad Mehdi</creatorcontrib><creatorcontrib>Jeddi-Tehrani, Mahmood</creatorcontrib><creatorcontrib>Kazemi, Tohid</creatorcontrib><creatorcontrib>Bahadori, Motahareh</creatorcontrib><creatorcontrib>Maddah, Mahshid</creatorcontrib><creatorcontrib>Hojjat-Farsangi, Mohammad</creatorcontrib><creatorcontrib>Khoshnoodi, Jalal</creatorcontrib><creatorcontrib>Rabbani, Hodjatallah</creatorcontrib><creatorcontrib>Shokri, Fazel</creatorcontrib><creatorcontrib>Dept of Oncology-Pathology</creatorcontrib><creatorcontrib>Karolinska Institutet</creatorcontrib><creatorcontrib>Inst för onkologi-patologi</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Immunology Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>UK & Ireland Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>SwePub</collection><collection>SwePub Articles</collection><collection>SWEPUB Freely available online</collection><collection>SwePub Articles full text</collection><jtitle>IMMUNOTHERAPY</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Amiri, Mohammad Mehdi</au><au>Jeddi-Tehrani, Mahmood</au><au>Kazemi, Tohid</au><au>Bahadori, Motahareh</au><au>Maddah, Mahshid</au><au>Hojjat-Farsangi, Mohammad</au><au>Khoshnoodi, Jalal</au><au>Rabbani, Hodjatallah</au><au>Shokri, Fazel</au><aucorp>Dept of Oncology-Pathology</aucorp><aucorp>Karolinska Institutet</aucorp><aucorp>Inst för onkologi-patologi</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Construction and characterization of a new chimeric antibody against HER2</atitle><jtitle>IMMUNOTHERAPY</jtitle><addtitle>Immunotherapy</addtitle><date>2013-07-01</date><risdate>2013</risdate><volume>5</volume><issue>7</issue><spage>703</spage><epage>715</epage><pages>703-715</pages><issn>1750-743X</issn><issn>1750-7448</issn><eissn>1750-7448</eissn><abstract>Immunotherapy with anti-HER2 antibodies has shown promising results in patients with HER2-positive breast cancer. We have recently reported characterization of a mouse monoclonal antibody (mAb) against HER2, which binds to an epitope different from that recognized by trastuzumab and specifically inhibits proliferation of tumor cells overexpressing HER2. In the present study we report chimerization of this antibody.
The immunoglobulin variable region heavy and light chain genes of 1T0 hybridoma cells were amplified and ligated to human -1 and constant region genes using splice overlap extension PCR. The chimeric antibody was subsequently expressed and characterized by ELISA, western blot and flow cytometry.
The purified chimeric antibody specifically binds to recombinant HER2 and HER2-overexpressing tumor cells and inhibits proliferation of these cells. The binding affinity of the chimeric mAb was comparable with the parental mouse mAb.
This chimeric anti-HER2 mAb is a potentially valuable tool for targeted immunotherapy.</abstract><cop>England</cop><pub>Future Medicine Ltd</pub><pmid>23829622</pmid><doi>10.2217/imt.13.67</doi><tpages>13</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | IMMUNOTHERAPY, 2013-07, Vol.5 (7), p.703-715 |
| issn | 1750-743X 1750-7448 1750-7448 |
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| subjects | Animals Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibodies, Monoclonal - therapeutic use Binding sites Biological activity Breast cancer Breast Neoplasms - immunology Breast Neoplasms - therapy Cancer och onkologi Care and treatment Cell Proliferation Chemical properties chimeric antibody Deoxyribonucleic acid DNA Enzyme-linked immunosorbent assay Female Genetic aspects Health aspects HER2 Humans Hybridomas Immunization, Passive - methods Immunodominant Epitopes - immunology Immunologi inom det medicinska området Kinases Klinisk medicin MEDICAL AND HEALTH SCIENCES MEDICIN OCH HÄLSOVETENSKAP Medicinska och farmaceutiska grundvetenskaper Mice Molecular Targeted Therapy Molecular weight Monoclonal antibodies monoclonal antibody Protein Engineering - methods Proteins Receptor, ErbB-2 - antagonists & inhibitors Receptor, ErbB-2 - immunology Recombinant Fusion Proteins - genetics Recombinant Fusion Proteins - immunology Recombinant Fusion Proteins - therapeutic use |
| title | Construction and characterization of a new chimeric antibody against HER2 |
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