Humanization and characterization of an anti-human TNF-α murine monoclonal antibody
A murine monoclonal antibody, m357, showing the highly neutralizing activities for human tumor necrosis factor (TNF-α) was chosen to be humanized by a variable domain resurfacing approach. The non-conserved surface residues in the framework regions of both the heavy and light chain variable regions...
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| Veröffentlicht in: | PloS one 2011-01, Vol.6 (1), p.e16373 |
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| description | A murine monoclonal antibody, m357, showing the highly neutralizing activities for human tumor necrosis factor (TNF-α) was chosen to be humanized by a variable domain resurfacing approach. The non-conserved surface residues in the framework regions of both the heavy and light chain variable regions were identified via a molecular modeling of m357 built by computer-assisted homology modeling. By replacing these critical surface residues with the human counterparts, a humanized version, h357, was generated. The humanized h357 IgG(1) was then stably expressed in a mammalian cell line and the purified antibody maintained the high antigen binding affinity as compared with the parental m357 based on a soluble TNF-α neutralization bioassay. Furthermore, h357 IgG(1) possesses the ability to mediate antibody-dependent cell-mediated cytotoxicity and complement dependent cytotoxicity upon binding to cells bearing the transmembrane form of TNF-α. In a mouse model of collagen antibody-induced arthritis, h357 IgG significantly inhibited disease progression by intra-peritoneal injection of 50 µg/mouse once-daily for 9 consecutive days. These results provided a basis for the development of h357 IgG as therapeutic use. |
| doi_str_mv | 10.1371/journal.pone.0016373 |
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The non-conserved surface residues in the framework regions of both the heavy and light chain variable regions were identified via a molecular modeling of m357 built by computer-assisted homology modeling. By replacing these critical surface residues with the human counterparts, a humanized version, h357, was generated. The humanized h357 IgG(1) was then stably expressed in a mammalian cell line and the purified antibody maintained the high antigen binding affinity as compared with the parental m357 based on a soluble TNF-α neutralization bioassay. Furthermore, h357 IgG(1) possesses the ability to mediate antibody-dependent cell-mediated cytotoxicity and complement dependent cytotoxicity upon binding to cells bearing the transmembrane form of TNF-α. In a mouse model of collagen antibody-induced arthritis, h357 IgG significantly inhibited disease progression by intra-peritoneal injection of 50 µg/mouse once-daily for 9 consecutive days. These results provided a basis for the development of h357 IgG as therapeutic use.</description><identifier>ISSN: 1932-6203</identifier><identifier>EISSN: 1932-6203</identifier><identifier>DOI: 10.1371/journal.pone.0016373</identifier><identifier>PMID: 21305012</identifier><language>eng</language><publisher>United States: Public Library of Science</publisher><subject>Amino acids ; Animals ; Antibodies, Monoclonal - genetics ; Antibodies, Monoclonal - immunology ; Antibody Affinity ; Antibody-dependent cell-mediated cytotoxicity ; Antigens ; Arthritis ; Arthritis, Experimental - drug therapy ; Binding ; Bioassays ; Biology ; Collagen ; Crohn's disease ; Crohns disease ; Crystallography ; Cytokines ; Cytotoxicity ; DNA polymerase ; Genetic engineering ; Health services ; Homology ; Humans ; Immunoglobulin G ; Immunoglobulins ; Immunology ; Laboratories ; Lupus ; Medicine ; Mice ; Modelling ; Models, Molecular ; Molecular modelling ; Monoclonal antibodies ; Mutagenesis, Site-Directed ; Neutralization ; Peritoneum ; Protein Engineering - methods ; Proteins ; Public health ; Residues ; Resurfacing ; Rheumatoid arthritis ; Surfacing ; Thermus aquaticus ; TNF inhibitors ; Toxicity ; Treatment Outcome ; Tumor Necrosis Factor-alpha - immunology ; Tumor necrosis factor-TNF ; Tumor necrosis factor-α</subject><ispartof>PloS one, 2011-01, Vol.6 (1), p.e16373</ispartof><rights>2011 Chiu et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License: https://creativecommons.org/licenses/by/4.0/ (the “License”), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><rights>Chiu et al. 2011</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-e3336cd9a16f85ddffb5724a2d11fdd054d0a0b74cdeb71301ec7e178f638c7c3</citedby><cites>FETCH-LOGICAL-c525t-e3336cd9a16f85ddffb5724a2d11fdd054d0a0b74cdeb71301ec7e178f638c7c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3031550/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC3031550/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,2100,2926,23865,27923,27924,53790,53792,79371,79372</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/21305012$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><contributor>Chin, Wei-Chun</contributor><creatorcontrib>Chiu, Wei-Chun</creatorcontrib><creatorcontrib>Lai, Ya-Ping</creatorcontrib><creatorcontrib>Chou, Min-Yuan</creatorcontrib><title>Humanization and characterization of an anti-human TNF-α murine monoclonal antibody</title><title>PloS one</title><addtitle>PLoS One</addtitle><description>A murine monoclonal antibody, m357, showing the highly neutralizing activities for human tumor necrosis factor (TNF-α) was chosen to be humanized by a variable domain resurfacing approach. The non-conserved surface residues in the framework regions of both the heavy and light chain variable regions were identified via a molecular modeling of m357 built by computer-assisted homology modeling. By replacing these critical surface residues with the human counterparts, a humanized version, h357, was generated. The humanized h357 IgG(1) was then stably expressed in a mammalian cell line and the purified antibody maintained the high antigen binding affinity as compared with the parental m357 based on a soluble TNF-α neutralization bioassay. Furthermore, h357 IgG(1) possesses the ability to mediate antibody-dependent cell-mediated cytotoxicity and complement dependent cytotoxicity upon binding to cells bearing the transmembrane form of TNF-α. In a mouse model of collagen antibody-induced arthritis, h357 IgG significantly inhibited disease progression by intra-peritoneal injection of 50 µg/mouse once-daily for 9 consecutive days. These results provided a basis for the development of h357 IgG as therapeutic use.</description><subject>Amino acids</subject><subject>Animals</subject><subject>Antibodies, Monoclonal - genetics</subject><subject>Antibodies, Monoclonal - immunology</subject><subject>Antibody Affinity</subject><subject>Antibody-dependent cell-mediated cytotoxicity</subject><subject>Antigens</subject><subject>Arthritis</subject><subject>Arthritis, Experimental - drug therapy</subject><subject>Binding</subject><subject>Bioassays</subject><subject>Biology</subject><subject>Collagen</subject><subject>Crohn's disease</subject><subject>Crohns disease</subject><subject>Crystallography</subject><subject>Cytokines</subject><subject>Cytotoxicity</subject><subject>DNA polymerase</subject><subject>Genetic engineering</subject><subject>Health services</subject><subject>Homology</subject><subject>Humans</subject><subject>Immunoglobulin G</subject><subject>Immunoglobulins</subject><subject>Immunology</subject><subject>Laboratories</subject><subject>Lupus</subject><subject>Medicine</subject><subject>Mice</subject><subject>Modelling</subject><subject>Models, Molecular</subject><subject>Molecular modelling</subject><subject>Monoclonal antibodies</subject><subject>Mutagenesis, Site-Directed</subject><subject>Neutralization</subject><subject>Peritoneum</subject><subject>Protein Engineering - methods</subject><subject>Proteins</subject><subject>Public health</subject><subject>Residues</subject><subject>Resurfacing</subject><subject>Rheumatoid arthritis</subject><subject>Surfacing</subject><subject>Thermus aquaticus</subject><subject>TNF inhibitors</subject><subject>Toxicity</subject><subject>Treatment Outcome</subject><subject>Tumor Necrosis Factor-alpha - immunology</subject><subject>Tumor necrosis factor-TNF</subject><subject>Tumor necrosis factor-α</subject><issn>1932-6203</issn><issn>1932-6203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2011</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>DOA</sourceid><recordid>eNp1Udtq3DAQFaUll23-oDSGPnujsSzJ-xIoS9MEQvqyfRZjXbJebGkr24Hkr_oj_aZqs96QPAQEEqNzzpyZQ8gXoHNgEi42YYwe2_k2eDunFAST7AM5gQUrclFQ9vHV-5ic9v2GUs4qIY7IcQGMcgrFCVldjx365gmHJvgMvcn0GiPqwcZDMbhUT2do8vUOnK3urvJ_f7NujI23WRd80G1IVp4xdTCPn8knh21vz6Z7Rn5f_Vgtr_PbXz9vlt9vc80LPuSWMSa0WSAIV3FjnKu5LEosDIAzhvLSUKS1LLWxtUyWwWppQVZOsEpLzWbkfK-7bUOvpoX0CopFmUYXiTIjN3uECbhR29h0GB9VwEY9F0K8VxiHRrdW2VJAhVZDWlJZlQ7twlChJRdOVDXsul1O3ca6s0ZbP0Rs34i-_fHNWt2HB8UoA85pEvg2CcTwZ7T98I7lco_SMfR9tO6lA1C1S_7AUrvk1ZR8on197e6FdIia_QeEPq55</recordid><startdate>20110131</startdate><enddate>20110131</enddate><creator>Chiu, Wei-Chun</creator><creator>Lai, Ya-Ping</creator><creator>Chou, Min-Yuan</creator><general>Public Library of Science</general><general>Public Library of Science (PLoS)</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>7QG</scope><scope>7QL</scope><scope>7QO</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7T5</scope><scope>7TG</scope><scope>7TM</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PDBOC</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>RC3</scope><scope>5PM</scope><scope>DOA</scope></search><sort><creationdate>20110131</creationdate><title>Humanization and characterization of an anti-human TNF-α murine monoclonal antibody</title><author>Chiu, Wei-Chun ; Lai, Ya-Ping ; Chou, Min-Yuan</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-e3336cd9a16f85ddffb5724a2d11fdd054d0a0b74cdeb71301ec7e178f638c7c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2011</creationdate><topic>Amino acids</topic><topic>Animals</topic><topic>Antibodies, Monoclonal - genetics</topic><topic>Antibodies, Monoclonal - immunology</topic><topic>Antibody Affinity</topic><topic>Antibody-dependent cell-mediated cytotoxicity</topic><topic>Antigens</topic><topic>Arthritis</topic><topic>Arthritis, Experimental - drug therapy</topic><topic>Binding</topic><topic>Bioassays</topic><topic>Biology</topic><topic>Collagen</topic><topic>Crohn's disease</topic><topic>Crohns disease</topic><topic>Crystallography</topic><topic>Cytokines</topic><topic>Cytotoxicity</topic><topic>DNA polymerase</topic><topic>Genetic engineering</topic><topic>Health services</topic><topic>Homology</topic><topic>Humans</topic><topic>Immunoglobulin G</topic><topic>Immunoglobulins</topic><topic>Immunology</topic><topic>Laboratories</topic><topic>Lupus</topic><topic>Medicine</topic><topic>Mice</topic><topic>Modelling</topic><topic>Models, Molecular</topic><topic>Molecular modelling</topic><topic>Monoclonal antibodies</topic><topic>Mutagenesis, Site-Directed</topic><topic>Neutralization</topic><topic>Peritoneum</topic><topic>Protein Engineering - 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The non-conserved surface residues in the framework regions of both the heavy and light chain variable regions were identified via a molecular modeling of m357 built by computer-assisted homology modeling. By replacing these critical surface residues with the human counterparts, a humanized version, h357, was generated. The humanized h357 IgG(1) was then stably expressed in a mammalian cell line and the purified antibody maintained the high antigen binding affinity as compared with the parental m357 based on a soluble TNF-α neutralization bioassay. Furthermore, h357 IgG(1) possesses the ability to mediate antibody-dependent cell-mediated cytotoxicity and complement dependent cytotoxicity upon binding to cells bearing the transmembrane form of TNF-α. In a mouse model of collagen antibody-induced arthritis, h357 IgG significantly inhibited disease progression by intra-peritoneal injection of 50 µg/mouse once-daily for 9 consecutive days. These results provided a basis for the development of h357 IgG as therapeutic use.</abstract><cop>United States</cop><pub>Public Library of Science</pub><pmid>21305012</pmid><doi>10.1371/journal.pone.0016373</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Amino acids Animals Antibodies, Monoclonal - genetics Antibodies, Monoclonal - immunology Antibody Affinity Antibody-dependent cell-mediated cytotoxicity Antigens Arthritis Arthritis, Experimental - drug therapy Binding Bioassays Biology Collagen Crohn's disease Crohns disease Crystallography Cytokines Cytotoxicity DNA polymerase Genetic engineering Health services Homology Humans Immunoglobulin G Immunoglobulins Immunology Laboratories Lupus Medicine Mice Modelling Models, Molecular Molecular modelling Monoclonal antibodies Mutagenesis, Site-Directed Neutralization Peritoneum Protein Engineering - methods Proteins Public health Residues Resurfacing Rheumatoid arthritis Surfacing Thermus aquaticus TNF inhibitors Toxicity Treatment Outcome Tumor Necrosis Factor-alpha - immunology Tumor necrosis factor-TNF Tumor necrosis factor-α |
| title | Humanization and characterization of an anti-human TNF-α murine monoclonal antibody |
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