ISSN:
1573-4943
Keywords:
scTcr
;
T-cell receptor
;
autoantibodies
;
circular dichroism
;
peptide mapping
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
Notes:
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 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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1023/A:1026361110795
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