Characterization and receptor specific toxicity of two diphtheria toxin‐related interleukin‐3 fusion proteins DAB389–mIL‐3 and DAB389–(Gly4Ser)2‐mIL‐3
We have constructed two fusion proteins, DAB389–mIL‐3 and DAB389‐(Gly4Ser)2–mIL‐3, in which the receptor‐binding domain of diphtheria toxin is replaced by mouse interleukin‐3 (IL‐3). Cytotoxic activity of the fusion toxins was observed on three out of six cell lines assayed. This toxicity was mediat...
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| Veröffentlicht in: | FEBS letters 1997-04, Vol.406 (1-2), p.157-161 |
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| creator | Liger, Dominique vanderSpek, Johanna C Gaillard, Carole Cansier, Christophe Murphy, John R Leboulch, Philippe Gillet, Daniel |
| description | We have constructed two fusion proteins, DAB389–mIL‐3 and DAB389‐(Gly4Ser)2–mIL‐3, in which the receptor‐binding domain of diphtheria toxin is replaced by mouse interleukin‐3 (IL‐3). Cytotoxic activity of the fusion toxins was observed on three out of six cell lines assayed. This toxicity was mediated through binding to the IL‐3 receptor as it was inhibited in a dose‐dependent manner with murine IL‐3 or anti‐IL‐3 neutralizing antibodies. DAB389–(Gly4Ser)2‐mIL‐3 was up to 5 times more toxic than DAB389–mIL‐3, depending on the cell line (0.8×10−10 M |
| doi_str_mv | 10.1016/S0014-5793(97)00243-3 |
| format | Article |
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Cytotoxic activity of the fusion toxins was observed on three out of six cell lines assayed. This toxicity was mediated through binding to the IL‐3 receptor as it was inhibited in a dose‐dependent manner with murine IL‐3 or anti‐IL‐3 neutralizing antibodies. DAB389–(Gly4Ser)2‐mIL‐3 was up to 5 times more toxic than DAB389–mIL‐3, depending on the cell line (0.8×10−10 M<IC50<3×10−10 M). These proteins can be used for the detection of IL‐3 receptors on mouse cells and should allow for the selective elimination of IL‐3 receptor‐positive pluripotent hematopoietic stem cells prior to bone marrow transplantation.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1016/S0014-5793(97)00243-3</identifier><identifier>PMID: 9109408</identifier><language>eng</language><publisher>England</publisher><subject>Animals ; Cell Line ; Cell Survival - drug effects ; Diphtheria toxin ; Diphtheria Toxin - chemistry ; Diphtheria Toxin - metabolism ; Diphtheria Toxin - toxicity ; Fusion toxin ; Interleukin-2 - chemistry ; Interleukin-2 - metabolism ; Interleukin-2 - toxicity ; Interleukin-3 ; Interleukin-3 - chemistry ; Interleukin-3 - metabolism ; Interleukin-3 - toxicity ; Mice ; Protein Folding ; Receptor targeting ; Receptors, Interleukin-3 - drug effects ; Receptors, Interleukin-3 - metabolism ; Recombinant Fusion Proteins - chemistry ; Recombinant Fusion Proteins - metabolism ; Recombinant Fusion Proteins - toxicity</subject><ispartof>FEBS letters, 1997-04, Vol.406 (1-2), p.157-161</ispartof><rights>FEBS Letters 406 (1997) 1873-3468 © 2015 Federation of European Biochemical Societies</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1016%2FS0014-5793%2897%2900243-3$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1016%2FS0014-5793%2897%2900243-3$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>315,781,785,1418,1434,27928,27929,45578,45579,46413,46837</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9109408$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Liger, Dominique</creatorcontrib><creatorcontrib>vanderSpek, Johanna C</creatorcontrib><creatorcontrib>Gaillard, Carole</creatorcontrib><creatorcontrib>Cansier, Christophe</creatorcontrib><creatorcontrib>Murphy, John R</creatorcontrib><creatorcontrib>Leboulch, Philippe</creatorcontrib><creatorcontrib>Gillet, Daniel</creatorcontrib><title>Characterization and receptor specific toxicity of two diphtheria toxin‐related interleukin‐3 fusion proteins DAB389–mIL‐3 and DAB389–(Gly4Ser)2‐mIL‐3</title><title>FEBS letters</title><addtitle>FEBS Lett</addtitle><description>We have constructed two fusion proteins, DAB389–mIL‐3 and DAB389‐(Gly4Ser)2–mIL‐3, in which the receptor‐binding domain of diphtheria toxin is replaced by mouse interleukin‐3 (IL‐3). Cytotoxic activity of the fusion toxins was observed on three out of six cell lines assayed. This toxicity was mediated through binding to the IL‐3 receptor as it was inhibited in a dose‐dependent manner with murine IL‐3 or anti‐IL‐3 neutralizing antibodies. DAB389–(Gly4Ser)2‐mIL‐3 was up to 5 times more toxic than DAB389–mIL‐3, depending on the cell line (0.8×10−10 M<IC50<3×10−10 M). These proteins can be used for the detection of IL‐3 receptors on mouse cells and should allow for the selective elimination of IL‐3 receptor‐positive pluripotent hematopoietic stem cells prior to bone marrow transplantation.</description><subject>Animals</subject><subject>Cell Line</subject><subject>Cell Survival - drug effects</subject><subject>Diphtheria toxin</subject><subject>Diphtheria Toxin - chemistry</subject><subject>Diphtheria Toxin - metabolism</subject><subject>Diphtheria Toxin - toxicity</subject><subject>Fusion toxin</subject><subject>Interleukin-2 - chemistry</subject><subject>Interleukin-2 - metabolism</subject><subject>Interleukin-2 - toxicity</subject><subject>Interleukin-3</subject><subject>Interleukin-3 - chemistry</subject><subject>Interleukin-3 - metabolism</subject><subject>Interleukin-3 - toxicity</subject><subject>Mice</subject><subject>Protein Folding</subject><subject>Receptor targeting</subject><subject>Receptors, Interleukin-3 - drug effects</subject><subject>Receptors, Interleukin-3 - metabolism</subject><subject>Recombinant Fusion Proteins - chemistry</subject><subject>Recombinant Fusion Proteins - metabolism</subject><subject>Recombinant Fusion Proteins - toxicity</subject><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1997</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kU1OwzAUhC0EgvJzBCQvyyJg57m1vWzLTytVYgGsLSexVUOaRI6rUlYcAYkrcLKehCStuvLzfOOx9Aaha0puKaHDuxdCKIsGXEJf8htCYgYRHKEeFbwZ2FAco97BcobO6_qdNHdB5Sk6lZRIRkQP_U0W2us0GO--dHBlgXWRYW9SU4XS47oyqbMuxaH8dKkLG1xaHNYlzly1CIvmle5Qsf3-8SbXwWTYFU1ablYfnQrYruo2t_JlMK6o8f1oDEJuv3-Xs3lnaH88iP2nfMNejL-JG7Z3XKITq_PaXO3PC_T2-PA6mUbz56fZZDSPqhgAIsq0ySxhYijilKUi1QkZJMOBIZJIYWwCNoaBSUCD4BxIJqCZG6MVNuOMwwW63uVWq2RpMlV5t9R-o_bbavh0x9cuN5sDpkS1jaiuEdWuW0muukYUqMeHcdyRFkjeyQD_zG2Ixw</recordid><startdate>19970407</startdate><enddate>19970407</enddate><creator>Liger, Dominique</creator><creator>vanderSpek, Johanna C</creator><creator>Gaillard, Carole</creator><creator>Cansier, Christophe</creator><creator>Murphy, John R</creator><creator>Leboulch, Philippe</creator><creator>Gillet, Daniel</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>19970407</creationdate><title>Characterization and receptor specific toxicity of two diphtheria toxin‐related interleukin‐3 fusion proteins DAB389–mIL‐3 and DAB389–(Gly4Ser)2‐mIL‐3</title><author>Liger, Dominique ; vanderSpek, Johanna C ; Gaillard, Carole ; Cansier, Christophe ; Murphy, John R ; Leboulch, Philippe ; Gillet, Daniel</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p2333-14aedf048682c4c8cab05b65e09098efb3f235eb3a387730d83b3a4c8f8fd7473</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1997</creationdate><topic>Animals</topic><topic>Cell Line</topic><topic>Cell Survival - drug effects</topic><topic>Diphtheria toxin</topic><topic>Diphtheria Toxin - chemistry</topic><topic>Diphtheria Toxin - metabolism</topic><topic>Diphtheria Toxin - toxicity</topic><topic>Fusion toxin</topic><topic>Interleukin-2 - chemistry</topic><topic>Interleukin-2 - metabolism</topic><topic>Interleukin-2 - toxicity</topic><topic>Interleukin-3</topic><topic>Interleukin-3 - chemistry</topic><topic>Interleukin-3 - metabolism</topic><topic>Interleukin-3 - toxicity</topic><topic>Mice</topic><topic>Protein Folding</topic><topic>Receptor targeting</topic><topic>Receptors, Interleukin-3 - drug effects</topic><topic>Receptors, Interleukin-3 - metabolism</topic><topic>Recombinant Fusion Proteins - chemistry</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>Recombinant Fusion Proteins - toxicity</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Liger, Dominique</creatorcontrib><creatorcontrib>vanderSpek, Johanna C</creatorcontrib><creatorcontrib>Gaillard, Carole</creatorcontrib><creatorcontrib>Cansier, Christophe</creatorcontrib><creatorcontrib>Murphy, John R</creatorcontrib><creatorcontrib>Leboulch, Philippe</creatorcontrib><creatorcontrib>Gillet, Daniel</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Liger, Dominique</au><au>vanderSpek, Johanna C</au><au>Gaillard, Carole</au><au>Cansier, Christophe</au><au>Murphy, John R</au><au>Leboulch, Philippe</au><au>Gillet, Daniel</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization and receptor specific toxicity of two diphtheria toxin‐related interleukin‐3 fusion proteins DAB389–mIL‐3 and DAB389–(Gly4Ser)2‐mIL‐3</atitle><jtitle>FEBS letters</jtitle><addtitle>FEBS Lett</addtitle><date>1997-04-07</date><risdate>1997</risdate><volume>406</volume><issue>1-2</issue><spage>157</spage><epage>161</epage><pages>157-161</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>We have constructed two fusion proteins, DAB389–mIL‐3 and DAB389‐(Gly4Ser)2–mIL‐3, in which the receptor‐binding domain of diphtheria toxin is replaced by mouse interleukin‐3 (IL‐3). Cytotoxic activity of the fusion toxins was observed on three out of six cell lines assayed. This toxicity was mediated through binding to the IL‐3 receptor as it was inhibited in a dose‐dependent manner with murine IL‐3 or anti‐IL‐3 neutralizing antibodies. DAB389–(Gly4Ser)2‐mIL‐3 was up to 5 times more toxic than DAB389–mIL‐3, depending on the cell line (0.8×10−10 M<IC50<3×10−10 M). These proteins can be used for the detection of IL‐3 receptors on mouse cells and should allow for the selective elimination of IL‐3 receptor‐positive pluripotent hematopoietic stem cells prior to bone marrow transplantation.</abstract><cop>England</cop><pmid>9109408</pmid><doi>10.1016/S0014-5793(97)00243-3</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | FEBS letters, 1997-04, Vol.406 (1-2), p.157-161 |
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| source | MEDLINE; Access via ScienceDirect (Elsevier); Wiley Online Library Free Content; Wiley Online Library All Journals; Alma/SFX Local Collection; EZB Electronic Journals Library |
| subjects | Animals Cell Line Cell Survival - drug effects Diphtheria toxin Diphtheria Toxin - chemistry Diphtheria Toxin - metabolism Diphtheria Toxin - toxicity Fusion toxin Interleukin-2 - chemistry Interleukin-2 - metabolism Interleukin-2 - toxicity Interleukin-3 Interleukin-3 - chemistry Interleukin-3 - metabolism Interleukin-3 - toxicity Mice Protein Folding Receptor targeting Receptors, Interleukin-3 - drug effects Receptors, Interleukin-3 - metabolism Recombinant Fusion Proteins - chemistry Recombinant Fusion Proteins - metabolism Recombinant Fusion Proteins - toxicity |
| title | Characterization and receptor specific toxicity of two diphtheria toxin‐related interleukin‐3 fusion proteins DAB389–mIL‐3 and DAB389–(Gly4Ser)2‐mIL‐3 |
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