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. 1994 Aug 30;91(18):8462–8466. doi: 10.1073/pnas.91.18.8462

Binding of a soluble alpha beta T-cell receptor to superantigen/major histocompatibility complex ligands.

J Kappler 1, J White 1, H Kozono 1, J Clements 1, P Marrack 1
PMCID: PMC44626  PMID: 8078904

Abstract

The genes for the alpha and beta 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 DR1 with the bacterial superantigen staphylococcal enterotoxin B.

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Selected References

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