-
- 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.
説明
<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>
収録刊行物
-
- Science
-
Science 266 (5192), 1874-1878, 1994-12-16
American Association for the Advancement of Science (AAAS)