Citation

Wagner K, Kwakkenbos MJ, Claassen YB, Maijoor K, Böhne M, van der Sluijs KF, Witte MD, van Zoelen DJ, Cornelissen LA, Beaumont T, Bakker AQ, Ploegh HL, Spits H. 2014. Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity. Proceedings of the National Academy of Sciences of the United States of America. 111(47):16820-5. Pubmed: 25385586 DOI:10.1073/pnas.1408605111

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.

Related Faculty

Photo of Hidde Ploegh

Hidde Ploegh studies molecular aspects of immune recognition, focusing on the use of nanobodies for non-invasive PET imaging to track immune responses.

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