Physical and epitope analysis of a recombinant human t-cell receptor Vα/Vβ construct support the similarity to immunoglobulin

Douglas Lake, Sam Helgerson, William J. Landsperger, John J. Marchalonis

Research output: Contribution to journalArticlepeer-review

Abstract

The genetic organization and protein structure of T-cell receptors (TCR) and immunoglobulins (Ig) are remarkably similar. Through recombinant, physical, and peptide-based immunological studies we demonstrated that rabbit antisera generated against a recombinant single-chain TCR (scTCR) react with defined peptide epitopes of their constituent TCR α and β chains. These antisera cross-react with the λ light-chain Meg as well as with peptides duplicating its covalent structure. Conversely, rabbit antisera generated to human λ light chains cross-reacted with the recombinant scTCR. Rabbit anti-λ antibodies purified on an scTCR affinity column bound to T-cell lines and to T and B lymphocytes from peripheral blood. Circular dichroism analysis demonstrated plots characteristic of β-sheets for both Meg and recombinant scTCR. Antisera directed against TCR α-chain synthetic peptides reacted with scTCR, Mcg λ light-chain protein, synthetic peptides from regions of sequence homology in β-chains, and Mcg. Based upon this homology and the serological cross-reactions which reflect conformational determinants, we suggest that the Vα/Vβ antigen-binding domain of this particular monoclonal scTCR construct is substantially similar to the conformational structure of λ light chains.

Original languageEnglish (US)
Pages (from-to)309-320
Number of pages12
JournalProtein Journal
Volume16
Issue number4
StatePublished - 1997
Externally publishedYes

Keywords

  • Autoantibodies
  • Circular dichroism
  • Peptide mapping
  • scTcr
  • T-cell receptor

ASJC Scopus subject areas

  • Biochemistry
  • Analytical Chemistry
  • Organic Chemistry
  • Bioengineering

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