tetano
Editor, Senior Moderator
Proc Natl Acad Sci U S A. 2014 Nov 10. pii: 201408605. [Epub ahead of print]
Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity.
Wagner K1, Kwakkenbos MJ1, Claassen YB1, Maijoor K1, B?hne M1, van der Sluijs KF2, Witte MD3, van Zoelen DJ4, Cornelissen LA4, Beaumont T1, Bakker AQ1, Ploegh HL3, Spits H5.
Author information
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
PMID:
25385586
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25385586
Bispecific antibody generated with sortase and click chemistry has broad antiinfluenza virus activity.
Wagner K1, Kwakkenbos MJ1, Claassen YB1, Maijoor K1, B?hne M1, van der Sluijs KF2, Witte MD3, van Zoelen DJ4, Cornelissen LA4, Beaumont T1, Bakker AQ1, Ploegh HL3, Spits H5.
Author information
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
PMID:
25385586
[PubMed - as supplied by publisher]
http://www.ncbi.nlm.nih.gov/pubmed/25385586