IgG-single-chain TRAIL fusion proteins for tumour therapy
Single-chain formats of TNF-related apoptosis inducing ligand (scTRAIL) can serve as effector components of tumour-associated antigen-targeted as well as non-targeted fusion proteins, being characterized by high tumour cell-specific induction of apoptosis through death receptor activation. We studie...
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| Veröffentlicht in: | Scientific reports 2018-05, Vol.8 (1), p.7808-11, Article 7808 |
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| creator | Siegemund, Martin Schneider, Felix Hutt, Meike Seifert, Oliver Müller, Ines Kulms, Dagmar Pfizenmaier, Klaus Kontermann, Roland E. |
| description | Single-chain formats of TNF-related apoptosis inducing ligand (scTRAIL) can serve as effector components of tumour-associated antigen-targeted as well as non-targeted fusion proteins, being characterized by high tumour cell-specific induction of apoptosis through death receptor activation. We studied the suitability of immunoglobulin G as a scaffold for oligovalent and bispecific TRAIL fusion proteins. Thus, we developed novel targeted hexa- and dodecavalent IgG-scTRAIL molecules by fusing scTRAIL to the C-terminus of either light (LC-scTRAIL) or heavy immunoglobulin chain (HC-scTRAIL), or to both ends (LC/HC-scTRAIL) of the anti-EGFR IgG antibody hu225. The binding specificity to EGFR and death receptors was retained in all IgG-scTRAIL formats and translated into high antigen-specific bioactivity on EGFR-positive Colo205, HCT116 and WM1366 tumour cell lines, with or without sensitization to apoptosis by bortezomib.
In vivo
, therapeutic potential was assessed for one of the targeted variants, HC-scTRAIL, compared to the non-targeted Fc-scTRAIL. Both molecules showed a significant reduction of tumour volume and synergism with a Smac mimetic in a Colo205 xenograft tumour model. The IgG-scTRAIL format allows directing a defined, highly bioactive form of TRAIL to a wide variety of tumour antigens, enabling customized solutions for a patient-specific targeted cancer therapy with a reduced risk of side effects. |
| doi_str_mv | 10.1038/s41598-018-24450-8 |
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In vivo
, therapeutic potential was assessed for one of the targeted variants, HC-scTRAIL, compared to the non-targeted Fc-scTRAIL. Both molecules showed a significant reduction of tumour volume and synergism with a Smac mimetic in a Colo205 xenograft tumour model. The IgG-scTRAIL format allows directing a defined, highly bioactive form of TRAIL to a wide variety of tumour antigens, enabling customized solutions for a patient-specific targeted cancer therapy with a reduced risk of side effects.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/s41598-018-24450-8</identifier><identifier>PMID: 29773864</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>13 ; 631/61/2297 ; 631/61/338/469 ; 631/67/1059/602 ; 64/60 ; 82 ; 82/1 ; 82/16 ; 82/80 ; 82/83 ; Antibodies, Monoclonal, Humanized - pharmacology ; Antigens ; Antineoplastic Agents - pharmacology ; Apoptosis ; Biological activity ; Bortezomib ; C-Terminus ; Cancer ; Cell Death - drug effects ; Cell Line, Tumor ; Death receptors ; DIABLO protein ; Epidermal growth factor receptors ; ErbB Receptors - immunology ; Humanities and Social Sciences ; Humans ; Immunoglobulin G ; Immunoglobulin G - chemistry ; Immunoglobulin G - pharmacology ; Immunoglobulins ; multidisciplinary ; Proteins ; Receptor mechanisms ; Recombinant Fusion Proteins - pharmacology ; Science ; Science (multidisciplinary) ; Synergism ; TNF-Related Apoptosis-Inducing Ligand - chemistry ; TNF-Related Apoptosis-Inducing Ligand - pharmacology ; TRAIL protein ; Tumor cell lines ; Tumor necrosis factor ; Tumors ; Xenografts</subject><ispartof>Scientific reports, 2018-05, Vol.8 (1), p.7808-11, Article 7808</ispartof><rights>The Author(s) 2018</rights><rights>2018. This work is published under http://creativecommons.org/licenses/by/4.0/ (the “License”). Notwithstanding the ProQuest Terms and Conditions, you may use this content in accordance with the terms of the License.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c474t-d538d487b193242d9dfab8d3a557a8b539a1d9acf1098102158980522f6c5f3f3</citedby><cites>FETCH-LOGICAL-c474t-d538d487b193242d9dfab8d3a557a8b539a1d9acf1098102158980522f6c5f3f3</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/PMC5958125/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC5958125/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27924,27925,41120,42189,51576,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29773864$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Siegemund, Martin</creatorcontrib><creatorcontrib>Schneider, Felix</creatorcontrib><creatorcontrib>Hutt, Meike</creatorcontrib><creatorcontrib>Seifert, Oliver</creatorcontrib><creatorcontrib>Müller, Ines</creatorcontrib><creatorcontrib>Kulms, Dagmar</creatorcontrib><creatorcontrib>Pfizenmaier, Klaus</creatorcontrib><creatorcontrib>Kontermann, Roland E.</creatorcontrib><title>IgG-single-chain TRAIL fusion proteins for tumour therapy</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>Single-chain formats of TNF-related apoptosis inducing ligand (scTRAIL) can serve as effector components of tumour-associated antigen-targeted as well as non-targeted fusion proteins, being characterized by high tumour cell-specific induction of apoptosis through death receptor activation. We studied the suitability of immunoglobulin G as a scaffold for oligovalent and bispecific TRAIL fusion proteins. Thus, we developed novel targeted hexa- and dodecavalent IgG-scTRAIL molecules by fusing scTRAIL to the C-terminus of either light (LC-scTRAIL) or heavy immunoglobulin chain (HC-scTRAIL), or to both ends (LC/HC-scTRAIL) of the anti-EGFR IgG antibody hu225. The binding specificity to EGFR and death receptors was retained in all IgG-scTRAIL formats and translated into high antigen-specific bioactivity on EGFR-positive Colo205, HCT116 and WM1366 tumour cell lines, with or without sensitization to apoptosis by bortezomib.
In vivo
, therapeutic potential was assessed for one of the targeted variants, HC-scTRAIL, compared to the non-targeted Fc-scTRAIL. Both molecules showed a significant reduction of tumour volume and synergism with a Smac mimetic in a Colo205 xenograft tumour model. The IgG-scTRAIL format allows directing a defined, highly bioactive form of TRAIL to a wide variety of tumour antigens, enabling customized solutions for a patient-specific targeted cancer therapy with a reduced risk of side effects.</description><subject>13</subject><subject>631/61/2297</subject><subject>631/61/338/469</subject><subject>631/67/1059/602</subject><subject>64/60</subject><subject>82</subject><subject>82/1</subject><subject>82/16</subject><subject>82/80</subject><subject>82/83</subject><subject>Antibodies, Monoclonal, Humanized - pharmacology</subject><subject>Antigens</subject><subject>Antineoplastic Agents - pharmacology</subject><subject>Apoptosis</subject><subject>Biological activity</subject><subject>Bortezomib</subject><subject>C-Terminus</subject><subject>Cancer</subject><subject>Cell Death - drug effects</subject><subject>Cell Line, Tumor</subject><subject>Death receptors</subject><subject>DIABLO protein</subject><subject>Epidermal growth factor receptors</subject><subject>ErbB Receptors - 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pharmacology</topic><topic>Antigens</topic><topic>Antineoplastic Agents - pharmacology</topic><topic>Apoptosis</topic><topic>Biological activity</topic><topic>Bortezomib</topic><topic>C-Terminus</topic><topic>Cancer</topic><topic>Cell Death - drug effects</topic><topic>Cell Line, Tumor</topic><topic>Death receptors</topic><topic>DIABLO protein</topic><topic>Epidermal growth factor receptors</topic><topic>ErbB Receptors - immunology</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>Immunoglobulin G</topic><topic>Immunoglobulin G - chemistry</topic><topic>Immunoglobulin G - pharmacology</topic><topic>Immunoglobulins</topic><topic>multidisciplinary</topic><topic>Proteins</topic><topic>Receptor mechanisms</topic><topic>Recombinant Fusion Proteins - pharmacology</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Synergism</topic><topic>TNF-Related Apoptosis-Inducing Ligand - chemistry</topic><topic>TNF-Related Apoptosis-Inducing Ligand - pharmacology</topic><topic>TRAIL protein</topic><topic>Tumor cell lines</topic><topic>Tumor necrosis factor</topic><topic>Tumors</topic><topic>Xenografts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Siegemund, Martin</creatorcontrib><creatorcontrib>Schneider, Felix</creatorcontrib><creatorcontrib>Hutt, Meike</creatorcontrib><creatorcontrib>Seifert, Oliver</creatorcontrib><creatorcontrib>Müller, Ines</creatorcontrib><creatorcontrib>Kulms, Dagmar</creatorcontrib><creatorcontrib>Pfizenmaier, Klaus</creatorcontrib><creatorcontrib>Kontermann, Roland E.</creatorcontrib><collection>Springer Nature OA Free Journals</collection><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>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</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>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</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>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content 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 Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Siegemund, Martin</au><au>Schneider, Felix</au><au>Hutt, Meike</au><au>Seifert, Oliver</au><au>Müller, Ines</au><au>Kulms, Dagmar</au><au>Pfizenmaier, Klaus</au><au>Kontermann, Roland E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>IgG-single-chain TRAIL fusion proteins for tumour therapy</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2018-05-17</date><risdate>2018</risdate><volume>8</volume><issue>1</issue><spage>7808</spage><epage>11</epage><pages>7808-11</pages><artnum>7808</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>Single-chain formats of TNF-related apoptosis inducing ligand (scTRAIL) can serve as effector components of tumour-associated antigen-targeted as well as non-targeted fusion proteins, being characterized by high tumour cell-specific induction of apoptosis through death receptor activation. We studied the suitability of immunoglobulin G as a scaffold for oligovalent and bispecific TRAIL fusion proteins. Thus, we developed novel targeted hexa- and dodecavalent IgG-scTRAIL molecules by fusing scTRAIL to the C-terminus of either light (LC-scTRAIL) or heavy immunoglobulin chain (HC-scTRAIL), or to both ends (LC/HC-scTRAIL) of the anti-EGFR IgG antibody hu225. The binding specificity to EGFR and death receptors was retained in all IgG-scTRAIL formats and translated into high antigen-specific bioactivity on EGFR-positive Colo205, HCT116 and WM1366 tumour cell lines, with or without sensitization to apoptosis by bortezomib.
In vivo
, therapeutic potential was assessed for one of the targeted variants, HC-scTRAIL, compared to the non-targeted Fc-scTRAIL. Both molecules showed a significant reduction of tumour volume and synergism with a Smac mimetic in a Colo205 xenograft tumour model. The IgG-scTRAIL format allows directing a defined, highly bioactive form of TRAIL to a wide variety of tumour antigens, enabling customized solutions for a patient-specific targeted cancer therapy with a reduced risk of side effects.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>29773864</pmid><doi>10.1038/s41598-018-24450-8</doi><tpages>11</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 13 631/61/2297 631/61/338/469 631/67/1059/602 64/60 82 82/1 82/16 82/80 82/83 Antibodies, Monoclonal, Humanized - pharmacology Antigens Antineoplastic Agents - pharmacology Apoptosis Biological activity Bortezomib C-Terminus Cancer Cell Death - drug effects Cell Line, Tumor Death receptors DIABLO protein Epidermal growth factor receptors ErbB Receptors - immunology Humanities and Social Sciences Humans Immunoglobulin G Immunoglobulin G - chemistry Immunoglobulin G - pharmacology Immunoglobulins multidisciplinary Proteins Receptor mechanisms Recombinant Fusion Proteins - pharmacology Science Science (multidisciplinary) Synergism TNF-Related Apoptosis-Inducing Ligand - chemistry TNF-Related Apoptosis-Inducing Ligand - pharmacology TRAIL protein Tumor cell lines Tumor necrosis factor Tumors Xenografts |
| title | IgG-single-chain TRAIL fusion proteins for tumour therapy |
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