Construction, purification and immunogenicity of antigen-antibody-LTB complexes

EA Green, Catherine Helen Botting, HM Webb, TR Hirst, Richard Edward Randall

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

An oligonucleotide, encoding a short epitope peptide tag, termed Pk, was inserted at the 3'-end of the gene coding B-subunit of Escherichia coli heat-labile enterotoxin (LTB). The presence of the Pk epitope on LTB-Pk was used to construct novel macromolecular assemblies comprising LTB-Pk, an anti-Pk mAb, (mAb SV5-P-k) and Pk-linked recombinant SIV proteins. The 1:1:1 stoichiometry of such complexes was ensured by binding LTB-Pk to one arm of mAb SV5-P-k and an SIV-Pk antigen to the other arm of the antibody. Such SIV-mAb-LTB macromolecular complexes bound to GM1-ganglioside in vitro, and when immunized systemically into mice were highly immunogenic, inducing both humoral and cell-mediated responses to the recombinant SIV antigens. Copyright (C) 1996 Elsevier Science Ltd.

Original languageEnglish
Pages (from-to)949-58
Number of pages10
JournalVaccine
Volume14
Issue number10
Publication statusPublished - Jul 1996

Keywords

  • LTB
  • immune complexes
  • immunotargeting
  • HEAT-LABILE ENTEROTOXIN
  • ESCHERICHIA-COLI ENTEROTOXINS
  • TOXIN B-SUBUNIT
  • VIBRIO-CHOLERAE
  • SIMIAN VIRUS-5
  • MARINE VIBRIO
  • EXTRACELLULAR PROTEINS
  • STRUCTURAL PROTEINS
  • IMMUNE-RESPONSES
  • SMAA COMPLEXES

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