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An Escherichia coli expression system has been developed to produce milligram quantities of the variable domains of a human T-cell receptor from a cytotoxic T cell that recognizes the HLA-A2-influenza matrix peptide complex as a single polypeptide chain. The recombinant protein was purified by metal-chelate chromatography and then refolded in a redox buffer system. The refolded protein was shown to directly bind both Staphylococcus aureus enterotoxin B and the major histocompatibility complex protein-peptide complex using a BIAcore biosensor. Thus this preparation of a single-chain, variable-domain, T-cell receptor fragment can bind both of its natural ligands and some of it is therefore a functional fragment of the receptor molecule.

Original publication

DOI

10.1073/pnas.91.19.9057

Type

Journal article

Journal

Proceedings of the National Academy of Sciences of the United States of America

Publication Date

09/1994

Volume

91

Pages

9057 - 9061

Addresses

Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.

Keywords

Humans, Escherichia coli, Receptors, Antigen, T-Cell, alpha-beta, Recombinant Proteins, Enterotoxins, HLA-A2 Antigen, Ligands, Biosensing Techniques, Amino Acid Sequence, Protein Binding, Solubility, Molecular Sequence Data