Prokaryotic production of the human T cell receptor V beta 2 chain and binding to toxic-shock syndrome toxin-1

The human T-cell receptor V beta 2-, D- and J-encoding domains were PCR-amplified from MOLT-4 total cDNA and subcloned in Escherichia coli. The V/D/J fragment was subsequently transferred to a prokaryotic expression vector in frame with a polyhistidine-encoding prosequence which enabled us to affinity-purify the fusion protein with IMAC (immobilized metal-ion affinity chromatorgraphy). Since the recombinant (re-) human T-cell receptor V beta 2 fusion protein (V beta 2 sol) produced in E. coli was found to be insoluble, purification was carried out under denaturating conditions. The purified and renatured re-protein, V beta 2 sol, was immunoreactive with an anti-V beta 2 monoclonal antibody in an ELISA assay. The specificity of V beta 2 sol was shown by its binding in vitro to the staphylococcal superantigen TSST-1, but not to the Staphylococcus aureus exotoxin-1 (SEA).