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

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

Research output: Contribution to journalArticle

11 Scopus citations

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 A light-chain Mcg 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 Mcg 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
JournalJournal of Protein Chemistry
Volume16
Issue number4
DOIs
StatePublished - Jun 20 1997
Externally publishedYes

Keywords

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

ASJC Scopus subject areas

  • Biochemistry

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