The assembly of single domain antibodies into bispecific decavalent molecules: J.Immunol.Methods

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TypeArticle
Journal titleJournal of Immunological Methods
Volume318
Issue1-2
Pages8894; # of pages: 7
SubjectAmino Acid Sequence; Animals; Antibodies; Antibodies,Bispecific; antibody; Antibody Affinity; Antigen-Antibody Reactions; biosynthesis; Camelids,New World; Canada; chemistry; Chromatography,Gel; DOMAIN; Form; Genetic Vectors; genetics; immunology; ISOLATION; Libraries; Linker; MODEL; Models,Molecular; Molecular Sequence Data; Molecular Weight; MOLECULE; Parathyroid Hormone-Related Protein; peptide; Peptide Fragments; protein; Protein Subunits; Recombinant Fusion Proteins; SEQUENCE; Shiga Toxins; SPECIFICITY; SUBUNIT; Surface Plasmon Resonance; verotoxin
AbstractBispecific antibodies present unique opportunities in terms of new applications for engineered antibodies. However, designing ideal bispecific antibodies remains a challenge. Here we describe a novel bispecific antibody model in which five single domain antibodies (sdAbs) are fused via a linker sequence to the N-terminus of the verotoxin B (VTB) subunit, a pentamerization domain, and five sdAbs are fused via a linker sequence to the VTB C-terminus. Fifteen such decavalent bispecific molecules, termed decabodies, were constructed and characterized for the purpose of identifying an optimal decabody design. One of the fifteen molecules existed in a non-aggregated decavalent form. In conjunction with the isolation of sdAbs with the desired specificities from non-immune phage display libraries, the decabody strategy provides a means of generating high avidity bispecific antibody reagents, with good physical properties, relatively quickly
Publication date
LanguageEnglish
AffiliationNRC Institute for Biological Sciences; National Research Council Canada
Peer reviewedNo
NRC numberSTONE2007
NPARC number9364909
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Record identifier11b4db95-274d-467e-aa47-e3d017eba8b2
Record created2009-07-10
Record modified2016-05-09
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