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The assembly of single domain antibodies into bispecific decavalent molecules

From National Research Council Canada

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FormatText, Article
Subjectamino acid sequence; 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
Abstract
Bispecific 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
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In
  • Journal of Immunological Methods 318, no. 1-2 (10 January 2007): 88–94.
LanguageEnglish
Peer reviewedYes
NRC numberSTONE2007
NPARC number9364909
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Record identifier11b4db95-274d-467e-aa47-e3d017eba8b2
Record created2009-07-10
Record modified2020-05-10
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