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. 1994 Sep 13;91(19):9057–9061. doi: 10.1073/pnas.91.19.9057

Binding of soluble natural ligands to a soluble human T-cell receptor fragment produced in Escherichia coli.

K L Hilyard 1, H Reyburn 1, S Chung 1, J I Bell 1, J L Strominger 1
PMCID: PMC44746  PMID: 8090768

Abstract

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.

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Selected References

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