Bispecific antibody generated with sortase and click chemistry has broad anti-influenza virus activity

K. Wagner, M.J. Kwakkenbos, Y.B. Claassen, K. Maijoor, M. Bohne, K.F. van der Sluijs, M.D. Witte, D.J. van Zoelen, A.H.M. Cornelissen, T. Beaumont, A.Q. Bakker, H.L. Ploegh, H.G. Spits

Research output: Contribution to journalArticleAcademicpeer-review

44 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)16820-16825
JournalProceedings of the National Academy of Sciences of the United States of America
Volume111
Issue number47
DOIs
Publication statusPublished - 2014

Keywords

  • influenza-a-viruses
  • memory b-cells
  • staphylococcus-aureus
  • human igg1
  • proteins
  • site
  • fab
  • binding
  • design
  • heterodimerization

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