Subsets of HLA-DR1 Molecules Defined by SEB and TSST-1 Binding

  • Jacques Thibodeau
    Laboratoire d'Immunologie, Institut de Recherches Cliniques de Montréal, Québec, Canada H2W 1 R7.
  • Isabelle Cloutier
    Laboratoire d'Immunologie, Institut de Recherches Cliniques de Montréal, Québec, Canada H2W 1 R7.
  • Pascal M. Lavoie
    Laboratoire d'Immunologie, Institut de Recherches Cliniques de Montréal, Québec, Canada H2W 1 R7.
  • Nathalie Labrecque
    Laboratoire d'Immunologie, Institut de Recherches Cliniques de Montréal, Québec, Canada H2W 1 R7.
  • Walid Mourad
    Département d'lmmunologie et de Rhumatologie, Centre Hospitalier de l'Université Laval, Sainte-Foy, Québec, Canada G1 V 4G2.
  • Theodore Jardetzky
    Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138, USA.
  • Rafick-Pierre Sékaly
    Laboratoire d'Immunologie, Institut de Recherches Cliniques de Montréal, Québec, Canada H2W 1 R7.

Description

<jats:p> Superantigens bind to major histocompatibility complex class II molecules on antigen-presenting cells and stimulate T cells. <jats:italic>Staphylococcus aureus</jats:italic> enterotoxin B (SEB) and toxic shock syndrome toxin-1 (TSST-1) bind to the same region of human lymphocyte antigen (HLA)-DR1 but do not compete with each other, which indicates that they bind to different subsets of DR1 molecules. Here, a mutation in the peptide-binding groove disrupted the SEB and TSST-1 binding sites, which suggests that peptides can influence the interaction with bacterial toxins. In support of this, the expression of the DR1 molecule in various cell types differentially affected the binding of these toxins. </jats:p>

Journal

  • Science

    Science 266 (5192), 1874-1878, 1994-12-16

    American Association for the Advancement of Science (AAAS)

Citations (1)*help

See more

Details 詳細情報について

Report a problem

Back to top