• Medientyp: E-Artikel
  • Titel: Specific Recognition of HLA-E, But Not Classical, HLA Class I Molecules by Soluble CD94/NKG2A and NK Cells
  • Beteiligte: Brooks, Andrew G.; Borrego, Francisco; Posch, Phillip E.; Patamawenu, Apisit; Scorzelli, Christopher J.; Ulbrecht, Matthias; Weiss, Elizabeth H.; Coligan, John E.
  • Erschienen: The American Association of Immunologists, 1999
  • Erschienen in: The Journal of Immunology
  • Sprache: Englisch
  • DOI: 10.4049/jimmunol.162.1.305
  • ISSN: 0022-1767; 1550-6606
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  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>The CD94/NKG2 receptors expressed by subpopulations of NK cells and T cells have been implicated as receptors for a broad range of both classical and nonclassical HLA class I molecules. To examine the ligand specificity of CD94/NKG2 proteins, a soluble heterodimeric form of the receptor was produced and used in direct binding studies with cells expressing defined HLA class I/peptide complexes. We confirm that CD94/NKG2A specifically interacts with HLA-E and demonstrate that this interaction is dependent on the association of HLA-E with peptide. Moreover, no interaction between CD94/NKG2A and classical HLA class I molecules was observed, as assayed by direct binding of the soluble receptor or by functional assays using CD94/NKG2A+ NK cells. The role of the peptide associated with HLA-E in the interaction between HLA-E and CD94/NKG2A was also assessed. All class I leader sequence peptides tested bound to HLA-E and were recognized by CD94/NKG2A. However, amino acid variations in class I leader sequences affected the stability of HLA-E. Additionally, not all HLA-E/peptide complexes examined were recognized by CD94/NKG2A. Thus CD94/NKG2A recognition of HLA-E is controlled by peptide at two levels; first, peptide must stabilize HLA-E and promote cell surface expression, and second, the HLA-E/peptide complex must form the ligand for CD94/NKG2A.</jats:p>
  • Zugangsstatus: Freier Zugang