Cutting edge: influence of the TCR V beta domain on the avidity of CD1d:alpha-galactosylceramide binding by invariant V alpha 14 NKT cells

J Immunol. 2003 Jun 15;170(12):5815-9. doi: 10.4049/jimmunol.170.12.5815.

Abstract

CD1d tetramers loaded with alpha-galactosylceramide (alpha-GalCer) bind selectively to mouse invariant Valpha14 (Valpha14i) NKT cells and their human counterparts. Whereas tetramer binding strictly depends on the expression of a Valpha14-Jalpha18 chain in murine NKT cells, the associated beta-chain (typically expressing Vbeta8.2 or Vbeta7) appears not to influence tetramer binding. In this study, we describe novel alpha-GalCer-loaded mouse and human CD1d-IgG1 dimers, which revealed an unexpected influence of the TCR-beta chain on the avidity of CD1d:alpha-GalCer binding. A subset of Valpha14i NKT cells clearly discriminated alpha-GalCer bound to mouse or human CD1d on the basis of avidity differences conferred by the Vbeta domain of the TCR-beta chain, with Vbeta8.2 conferring higher avidity binding than Vbeta7.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Antigens, CD1 / metabolism*
  • Antigens, CD1d
  • Cell Adhesion / immunology
  • Dimerization
  • Dose-Response Relationship, Immunologic
  • Galactosylceramides / metabolism*
  • Humans
  • Killer Cells, Natural / immunology*
  • Killer Cells, Natural / metabolism*
  • Mice
  • Mice, Inbred C57BL
  • Peptide Fragments / physiology*
  • Protein Structure, Tertiary
  • Receptors, Antigen, T-Cell, alpha-beta / physiology*
  • T-Lymphocyte Subsets / immunology*
  • T-Lymphocyte Subsets / metabolism*
  • Tumor Cells, Cultured

Substances

  • Antigens, CD1
  • Antigens, CD1d
  • CD1D protein, human
  • Galactosylceramides
  • Peptide Fragments
  • Receptors, Antigen, T-Cell, alpha-beta
  • T-cell receptor Vbeta 8.2