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Cutting edge: trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC:peptide ligands.

Publication ,  Journal Article
Redpath, S; Alam, SM; Lin, CM; O'Rourke, AM; Gascoigne, NR
Published in: J Immunol
July 1, 1999

Bacterial superantigens such as Staphylococcus aureus enterotoxin A (SEA) are very potent stimulators of T cells. They bind to the Vbeta region of the TCR and to MHC class II, stimulating T cells at nanomolar concentrations. Using surface plasmon resonance measurements, we find that binding between the individual components of the complex (TCR-class II, TCR-SEA, SEA-class II) is very weak, but that the stability of the trimolecular complex is considerably enhanced, reaching an affinity similar to that found for TCR interactions with MHC:peptide ligand. Thus, the potency of SEA in stimulation of T cells is not due to particularly strong affinities between the proteins, but to a cooperative effect of interactions in the TCR-SEA-MHC class II trimolecular complex that brings the kinetics into a similar range to binding of conventional Ags. This range may be the optimum for T cell activation.

Duke Scholars

Published In

J Immunol

ISSN

0022-1767

Publication Date

July 1, 1999

Volume

163

Issue

1

Start / End Page

6 / 10

Location

United States

Related Subject Headings

  • Surface Plasmon Resonance
  • Superantigens
  • Solubility
  • Signaling Lymphocytic Activation Molecule Family
  • Receptors, Immunologic
  • Receptors, Antigen, T-Cell, alpha-beta
  • Protein Binding
  • Peptide Fragments
  • Mice
  • Membrane Glycoproteins
 

Citation

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Redpath, S., Alam, S. M., Lin, C. M., O’Rourke, A. M., & Gascoigne, N. R. (1999). Cutting edge: trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC:peptide ligands. J Immunol, 163(1), 6–10.
Redpath, S., S. M. Alam, C. M. Lin, A. M. O’Rourke, and N. R. Gascoigne. “Cutting edge: trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC:peptide ligands.J Immunol 163, no. 1 (July 1, 1999): 6–10.
Redpath S, Alam SM, Lin CM, O’Rourke AM, Gascoigne NR. Cutting edge: trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC:peptide ligands. J Immunol. 1999 Jul 1;163(1):6–10.
Redpath S, Alam SM, Lin CM, O’Rourke AM, Gascoigne NR. Cutting edge: trimolecular interaction of TCR with MHC class II and bacterial superantigen shows a similar affinity to MHC:peptide ligands. J Immunol. 1999 Jul 1;163(1):6–10.

Published In

J Immunol

ISSN

0022-1767

Publication Date

July 1, 1999

Volume

163

Issue

1

Start / End Page

6 / 10

Location

United States

Related Subject Headings

  • Surface Plasmon Resonance
  • Superantigens
  • Solubility
  • Signaling Lymphocytic Activation Molecule Family
  • Receptors, Immunologic
  • Receptors, Antigen, T-Cell, alpha-beta
  • Protein Binding
  • Peptide Fragments
  • Mice
  • Membrane Glycoproteins