Secretion of T cell receptor fragments from recombinant Escherichia coli cells.
This study describes the secretion and purification of T cell receptor (TCR) V alpha, V beta domains and single chain V alpha-V beta fragments (scTCRs) from recombinant Escherichia coli cells. The TCR V alpha and V beta genes are derived from a T cell hybridoma that is associated with disease pathogenesis in murine experimental allergic encephalomyelitis (EAE). Circular dichroism (c.d.) analyses of the single domains and the scTCR indicate that they are folded into beta-pleated sheet structures similar to those of immunoglobulin variable domains. The secreted TCR fragments can be purified in milligram quantities, and could therefore be used in high-resolution structural studies, in immunization to generate anti-clonotypic antibodies or in vaccination.
Ward
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Cancer Immunobiology Center, University of Texas Southwestern Medical Center, Dallas 75235-8576.
D000818:Animals; D001483:Base Sequence; D002942:Circular Dichroism; D004681:Encephalomyelitis, Autoimmune, Experimental / Q000276:immunology; D004926:Escherichia coli; D006860:Hydrogen Bonding; D051379:Mice; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016693:Receptors, Antigen, T-Cell, alpha-beta / Q000378:metabolism* / Q000648:ultrastructure; D011994:Recombinant Proteins / Q000378:metabolism* / Q000648:ultrastructure
D016693:Receptors, Antigen, T-Cell, alpha-beta; D011994:Recombinant Proteins