| Literature DB >> 25385586 |
Koen Wagner1, Mark J Kwakkenbos1, Yvonne B Claassen1, Kelly Maijoor1, Martino Böhne1, Koenraad F van der Sluijs2, Martin D Witte3, Diana J van Zoelen4, Lisette A Cornelissen4, Tim Beaumont1, Arjen Q Bakker1, Hidde L Ploegh3, Hergen Spits5.
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.Keywords: antibody engineering; immunotherapy; influenza
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Year: 2014 PMID： 25385586 PMCID： PMC4250106 DOI： 10.1073/pnas.1408605111
Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205