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The identification of tyrosine as a common key residue in unrelated H-2Kd restricted antigenic peptides

Maryanski, Janet L. ; Romero, Pedro ; Van Pel, Aline ; Boon, Thierry ; Salemme, F. R. ; Cerottini, Jean-Charles ; Corradin, Giampietro

In: International Immunology, 1991, vol. 3, no. 10, p. 1035-1042

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    Titel
    • The identification of tyrosine as a common key residue in unrelated H-2Kd restricted antigenic peptides
    Autor
    • Maryanski, Janet L.. Correspondence to: J. L. Maryanski, Ludwig Institute for Cancer Research, Ch. des Boveresses 155, 1066 Epalinges, Switzerland
    • Romero, Pedro
    • Van Pel, Aline. Ludwig Institute for Cancer Research, Brussels Branch 74 avenue Hippocrate, B-1200 Brussels, Belgium
    • Boon, Thierry. Ludwig Institute for Cancer Research, Brussels Branch 74 avenue Hippocrate, B-1200 Brussels, Belgium
    • Salemme, F. R.. Central Research and Development Department, Dupont Experimental Station ES228/320 Wilmington, DE 19880-0228, USA
    • Cerottini, Jean-Charles
    • Corradin, Giampietro. Institute of Biochemistry, University of Lausanne 1066 Epalinges, Switzerland
    Dokumententyp
    • Postprint
    Sprache
    • Englisch
    Veröffentlicht in
    • International Immunology, 1991, vol. 3, no. 10, p. 1035-1042. Oxford University Press
    Andere elektronische Ausgabe
    OAI-PMH-ID
    • oai:doc.rero.ch:299354
    Summary
    we have compared the activity of several Kd-or Ld-restricted antigenic peptides as competitors in a functional competition assay using cytolytic T lymphocyte (CTL) clones. All of four unrelated Kd-restricted peptides tested could compete with each other but not with the Ld-restricted peptide P91A-.12-24 (P91A). Moreover, the P91A peptide falled to compete with the four Kd-restricted peptides. In contrast, another Ld-restricted peptide[mouse cytomegalovirus (MCMV) pp89 167-176] could clearly compete with both Kd- and Ld-restricted peptides. The comparison of a series of modified MCMV pp89 peptides suggested that distinct structural features allow the Interaction of the peptide with the two different MHC class I molecules. We showed previously that the competitor activity of two different Kd-restricted antigenic peptides was reduced substantially upon Ala substitution of the single Tyr residues present in these peptides. We now show a similar effect for two additional Kd-restricted peptides. Our results thus suggest that Tyr may function as an ‘anchor' residue for many antigentic peptides that bind to the Kdmolecule. Molecular modeling of the presumed antigen-binding site of the Kdmolecule revealed the presence of two deep cavities that may be involved in binding peptide amino acid side chains. A model Illustrating one possible interaction of a Tyr-containing peptide with the Kdmolecule is presented