Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity
Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains...
| Main Authors: | , , , , , , , , , , , , |
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| Format: | Article |
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National Academy of Sciences (U.S.)
2018
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| Online Access: | http://hdl.handle.net/1721.1/115434 https://orcid.org/0000-0002-1090-6071 |
| _version_ | 1826191066524549120 |
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| author | Wagner, Koen Kwakkenbos, Mark J. Claassen, Yvonne B. Maijoor, Kelly Böhne, Martino van der Sluijs, Koenraad F. Witte, Martin D. van Zoelen, Diana J. Cornelissen, Lisette A. Beaumont, Tim Bakker, Arjen Q. Spits, Hergen Ploegh, Hidde |
| author2 | Massachusetts Institute of Technology. Department of Biology |
| author_facet | Massachusetts Institute of Technology. Department of Biology Wagner, Koen Kwakkenbos, Mark J. Claassen, Yvonne B. Maijoor, Kelly Böhne, Martino van der Sluijs, Koenraad F. Witte, Martin D. van Zoelen, Diana J. Cornelissen, Lisette A. Beaumont, Tim Bakker, Arjen Q. Spits, Hergen Ploegh, Hidde |
| author_sort | Wagner, Koen |
| collection | MIT |
| description | Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains into a single molecule. Here, we present a bispecific format where we have fused two full-sized IgG antibodies via their C termini using sortase transpeptidation and click chemistry to create a covalently linked IgG antibody heterodimer. By linking two potent anti-influenza A antibodies together, we have generated a full antibody dimer with bispecific activity that retains the activity and stability of the two fusion partners. |
| first_indexed | 2024-09-23T08:49:38Z |
| format | Article |
| id | mit-1721.1/115434 |
| institution | Massachusetts Institute of Technology |
| last_indexed | 2024-09-23T08:49:38Z |
| publishDate | 2018 |
| publisher | National Academy of Sciences (U.S.) |
| record_format | dspace |
| spelling | mit-1721.1/1154342022-09-30T11:34:11Z Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity Wagner, Koen Kwakkenbos, Mark J. Claassen, Yvonne B. Maijoor, Kelly Böhne, Martino van der Sluijs, Koenraad F. Witte, Martin D. van Zoelen, Diana J. Cornelissen, Lisette A. Beaumont, Tim Bakker, Arjen Q. Spits, Hergen Ploegh, Hidde Massachusetts Institute of Technology. Department of Biology Ploegh, Hidde Bispecific antibodies have therapeutic potential by expanding the functions of conventional antibodies. Many different formats of bispecific antibodies have meanwhile been developed. Most are genetic modifications of the antibody backbone to facilitate incorporation of two different variable domains into a single molecule. Here, we present a bispecific format where we have fused two full-sized IgG antibodies via their C termini using sortase transpeptidation and click chemistry to create a covalently linked IgG antibody heterodimer. By linking two potent anti-influenza A antibodies together, we have generated a full antibody dimer with bispecific activity that retains the activity and stability of the two fusion partners. 2018-05-17T18:20:15Z 2018-05-17T18:20:15Z 2014-11 2018-05-10T16:11:22Z Article http://purl.org/eprint/type/JournalArticle 0027-8424 1091-6490 http://hdl.handle.net/1721.1/115434 Wagner, Koen et al. “Bispecific Antibody Generated with Sortase and Click Chemistry Has Broad Antiinfluenza Virus Activity.” Proceedings of the National Academy of Sciences 111, 47 (November 2014): 16820–16825 https://orcid.org/0000-0002-1090-6071 http://dx.doi.org/10.1073/PNAS.1408605111 Proceedings of the National Academy of Sciences Article is made available in accordance with the publisher's policy and may be subject to US copyright law. Please refer to the publisher's site for terms of use. application/pdf National Academy of Sciences (U.S.) PNAS |
| spellingShingle | Wagner, Koen Kwakkenbos, Mark J. Claassen, Yvonne B. Maijoor, Kelly Böhne, Martino van der Sluijs, Koenraad F. Witte, Martin D. van Zoelen, Diana J. Cornelissen, Lisette A. Beaumont, Tim Bakker, Arjen Q. Spits, Hergen Ploegh, Hidde Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| title | Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| title_full | Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| title_fullStr | Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| title_full_unstemmed | Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| title_short | Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| title_sort | bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity |
| url | http://hdl.handle.net/1721.1/115434 https://orcid.org/0000-0002-1090-6071 |
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