Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity
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16820.full.pdf
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Checksum (MD5)
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Author(s)
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
Date Issued
November 2014
Journal
Proceedings of the National Academy of Sciences
Publisher
National Academy of Sciences (U.S.)
Citation
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
Version
Final published version
Abstract
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.
MIT Department
Massachusetts Institute of Technology. Department of Biology
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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.
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DOI of Published Version
https://doi.org/10.1073/PNAS.1408605111
