Expression and Characterization of a Divalent Chimeric Anti‐Human CD3 Single Chain Antibody
Murine anti‐CD3 monoclonal antibodies (MoAbs) are used in clinical practice for immunosuppression. However, there are two major drawbacks to this treatment: the associated cytokine release syndrome and human anti‐mouse antibody response. To overcome these side‐effects, the authors generated a chimer...
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| Veröffentlicht in: | Scandinavian journal of immunology 1996-02, Vol.43 (2), p.134-139 |
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| container_title | Scandinavian journal of immunology |
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| creator | MA, SHENGLIN THOMPSON, J. HU, HUAIZHONG NEVILLE JR, D. M. |
| description | Murine anti‐CD3 monoclonal antibodies (MoAbs) are used in clinical practice for immunosuppression. However, there are two major drawbacks to this treatment: the associated cytokine release syndrome and human anti‐mouse antibody response. To overcome these side‐effects, the authors generated a chimeric anti‐human CD3 single chain antibody, scUCHT1. It is an IgM variant of UCHT1, a mouse IgG1 MoAb directed against human CD3. scUCHT1 consists of the light and heavy variable chain binding domains of UCHT1 and a human IgM Fc region (CH2 to CH4). scUCHT1 was produced by COS‐7 and SP2/0 transfectants, and mainly assembled in a dimeric form. It retained the binding specificity and affinity of the parental MoAb UCHT1. In contrast to UCHT1, scUCHT1 did not induce T‐cell proliferation and cytokine release (TNF‐α and IFN‐γ) in in vitro assays. These results suggest that the engineered chimeric anti‐CD3 single chain antibody (scUCHT1) may be useful in clinical immunosuppressive treatment. |
| doi_str_mv | 10.1046/j.1365-3083.1996.d01-22.x |
| format | Article |
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M.</creatorcontrib><title>Expression and Characterization of a Divalent Chimeric Anti‐Human CD3 Single Chain Antibody</title><title>Scandinavian journal of immunology</title><addtitle>Scand J Immunol</addtitle><description>Murine anti‐CD3 monoclonal antibodies (MoAbs) are used in clinical practice for immunosuppression. However, there are two major drawbacks to this treatment: the associated cytokine release syndrome and human anti‐mouse antibody response. To overcome these side‐effects, the authors generated a chimeric anti‐human CD3 single chain antibody, scUCHT1. It is an IgM variant of UCHT1, a mouse IgG1 MoAb directed against human CD3. scUCHT1 consists of the light and heavy variable chain binding domains of UCHT1 and a human IgM Fc region (CH2 to CH4). scUCHT1 was produced by COS‐7 and SP2/0 transfectants, and mainly assembled in a dimeric form. It retained the binding specificity and affinity of the parental MoAb UCHT1. In contrast to UCHT1, scUCHT1 did not induce T‐cell proliferation and cytokine release (TNF‐α and IFN‐γ) in in vitro assays. These results suggest that the engineered chimeric anti‐CD3 single chain antibody (scUCHT1) may be useful in clinical immunosuppressive treatment.</description><subject>Animals</subject><subject>Antibodies, Monoclonal - chemistry</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - pharmacology</subject><subject>Antibody Affinity</subject><subject>Antibody Specificity</subject><subject>Base Sequence</subject><subject>CD3 Complex - immunology</subject><subject>Genetic Vectors</subject><subject>Humans</subject><subject>Immunoglobulin M - chemistry</subject><subject>Immunoglobulin M - genetics</subject><subject>Immunoglobulin M - isolation & purification</subject><subject>Interferon-gamma - biosynthesis</subject><subject>Lymphocyte Activation</subject><subject>Mice</subject><subject>Molecular Sequence Data</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - isolation & purification</subject><subject>Recombinant Fusion Proteins - pharmacology</subject><subject>T-Lymphocytes - immunology</subject><subject>Tumor Necrosis Factor-alpha - biosynthesis</subject><issn>0300-9475</issn><issn>1365-3083</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1996</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkU1u2zAQhYkiReK6PUIBZZOdVJJDUiKQjeGkcYoAXSRZFgRFjRoa-nFEObG7yhF6xpwkUm14m64GmO-9GeA9Qk4ZTRgV6tsyYaBkDDSDhGmtkoKymPNk84FMDuSITChQGmuRyhPyKYQlpQx4CsfkOFMATPMJ-XW5WXUYgm-byDZFNH-wnXU9dv6P7cdlW0Y2uvBPtsKmH7CvB-aiWdP715e_i3Vtm2h-AdGtb35XOPp984_mbbH9TD6Wtgr4ZT-n5P775d18Ed_8vLqez25iB1rxmOUcec5ZrnKkhdRQIEup1BpchghSIJOc55krS5nRTEghQZWsEI4LJ3QOU3K2u7vq2sc1ht7UPjisKttguw4mzagAoeS7QiZlmoESg1DvhK5rQ-iwNKvO17bbGkbN2IFZmjFpMyZtxg7M0IHh3GwG79f9k3VeY3Fw7kMf-PmOP_sKt_9_2Nz-uAYOb6uRlaU</recordid><startdate>199602</startdate><enddate>199602</enddate><creator>MA, SHENGLIN</creator><creator>THOMPSON, J.</creator><creator>HU, HUAIZHONG</creator><creator>NEVILLE JR, D. 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M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c3962-1b2e2b21b6be0d593de1705993c8ee354e1522b8cff5808454536f1d4c24c49b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1996</creationdate><topic>Animals</topic><topic>Antibodies, Monoclonal - chemistry</topic><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibodies, Monoclonal - pharmacology</topic><topic>Antibody Affinity</topic><topic>Antibody Specificity</topic><topic>Base Sequence</topic><topic>CD3 Complex - immunology</topic><topic>Genetic Vectors</topic><topic>Humans</topic><topic>Immunoglobulin M - chemistry</topic><topic>Immunoglobulin M - genetics</topic><topic>Immunoglobulin M - isolation & purification</topic><topic>Interferon-gamma - biosynthesis</topic><topic>Lymphocyte Activation</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - isolation & purification</topic><topic>Recombinant Fusion Proteins - pharmacology</topic><topic>T-Lymphocytes - immunology</topic><topic>Tumor Necrosis Factor-alpha - biosynthesis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>MA, SHENGLIN</creatorcontrib><creatorcontrib>THOMPSON, J.</creatorcontrib><creatorcontrib>HU, HUAIZHONG</creatorcontrib><creatorcontrib>NEVILLE JR, D. M.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Immunology Abstracts</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Scandinavian journal of immunology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>MA, SHENGLIN</au><au>THOMPSON, J.</au><au>HU, HUAIZHONG</au><au>NEVILLE JR, D. M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Expression and Characterization of a Divalent Chimeric Anti‐Human CD3 Single Chain Antibody</atitle><jtitle>Scandinavian journal of immunology</jtitle><addtitle>Scand J Immunol</addtitle><date>1996-02</date><risdate>1996</risdate><volume>43</volume><issue>2</issue><spage>134</spage><epage>139</epage><pages>134-139</pages><issn>0300-9475</issn><eissn>1365-3083</eissn><abstract>Murine anti‐CD3 monoclonal antibodies (MoAbs) are used in clinical practice for immunosuppression. However, there are two major drawbacks to this treatment: the associated cytokine release syndrome and human anti‐mouse antibody response. To overcome these side‐effects, the authors generated a chimeric anti‐human CD3 single chain antibody, scUCHT1. It is an IgM variant of UCHT1, a mouse IgG1 MoAb directed against human CD3. scUCHT1 consists of the light and heavy variable chain binding domains of UCHT1 and a human IgM Fc region (CH2 to CH4). scUCHT1 was produced by COS‐7 and SP2/0 transfectants, and mainly assembled in a dimeric form. It retained the binding specificity and affinity of the parental MoAb UCHT1. In contrast to UCHT1, scUCHT1 did not induce T‐cell proliferation and cytokine release (TNF‐α and IFN‐γ) in in vitro assays. These results suggest that the engineered chimeric anti‐CD3 single chain antibody (scUCHT1) may be useful in clinical immunosuppressive treatment.</abstract><cop>Oxford, U.K. and Cambridge, USA</cop><pub>Blackwell Science Ltd</pub><pmid>8633192</pmid><doi>10.1046/j.1365-3083.1996.d01-22.x</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0300-9475 |
| ispartof | Scandinavian journal of immunology, 1996-02, Vol.43 (2), p.134-139 |
| issn | 0300-9475 1365-3083 |
| language | eng |
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| source | MEDLINE; Wiley Online Library Journals Frontfile Complete |
| subjects | Animals Antibodies, Monoclonal - chemistry Antibodies, Monoclonal - genetics Antibodies, Monoclonal - pharmacology Antibody Affinity Antibody Specificity Base Sequence CD3 Complex - immunology Genetic Vectors Humans Immunoglobulin M - chemistry Immunoglobulin M - genetics Immunoglobulin M - isolation & purification Interferon-gamma - biosynthesis Lymphocyte Activation Mice Molecular Sequence Data Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - isolation & purification Recombinant Fusion Proteins - pharmacology T-Lymphocytes - immunology Tumor Necrosis Factor-alpha - biosynthesis |
| title | Expression and Characterization of a Divalent Chimeric Anti‐Human CD3 Single Chain Antibody |
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