Binding of a soluble αβ T-cell receptor to superantigen/major histocompatibility complex ligands

Abstract

The genes for the α and β chains of a murine T-cell receptor were truncated just prior to the portions encoding the transmembrane regions and introduced into baculovirus by recombination. Insect cells infected with the virus secreted a soluble form of the receptor that could be purified to homogeneity. This soluble receptor reacted with a set of six monoclonal antibodies originally raised to different epitopes on the natural transmembrane-region-containing receptor and bound with appropriate specificity to a cell surface complex of the human major histocompatibility complex class II molecule DRI with the bacterial superantigen staphylococcal enterotoxin B.