Secretion of a chimeric T-cell receptor-immunoglobulin protein.
AUTOR(ES)
Gascoigne, N R
RESUMO
To produce sufficient quantities of soluble T-cell receptor protein for detailed biochemical and biophysical analyses we have explored the use of immunoglobulin--T-cell receptor gene fusions. In this report we describe a chimeric gene construct containing a T-cell receptor alpha-chain variable (V) domain and the constant (C) region coding sequences of an immunoglobulin gamma 2a molecule. Cells transfected with the chimeric gene synthesize a stable protein product that expresses immunoglobulin and T-cell receptor antigenic determinants as well as protein A binding sites. We show that the determinant recognized by the anticlonotypic antibody A2B4.2 resides on the V alpha domain of the T-cell receptor. The chimeric protein associates with a normal lambda light chain to form an apparently normal tetrameric (H2L2, where H = heavy and L = light) immunoglobulin molecule that is secreted. Also of potential significance is the fact that a T-cell receptor V beta gene in the same construct is neither assembled nor secreted with the lambda light chain, and when expressed with a C kappa region it does not assemble with the chimeric V alpha C gamma 2a protein mentioned above. This indicates that not all T-cell receptor V regions are similar enough to immunoglobulin V regions for them to be completely interchangeable.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=304775Documentos Relacionados
- Secretion of a soluble, chimeric gamma delta T-cell receptor-immunoglobulin heterodimer.
- T-cell receptor genes in autoimmune mice: T-cell subsets have unexpected T-cell receptor gene programs.
- Regulation of T-cell receptor gene expression in human T-cell development.
- T-cell specific rearrangement of T-cell receptor beta transgenes in mice.
- Rearrangement of T-cell receptor beta-chain genes during T-cell development.