Activation of T cells by the ragged tail of MHC class II-presented peptides of the measles virus fusion protein

Claude P. Muller*, Wim Ammerlaan, Burkhard Fleckenstein, Steffen Krauss, Hubert Kalbacher, Francois Schneider, Günther Jung, Karl Heinz Wiesmüller

*Corresponding author for this work

    Research output: Contribution to journalArticleResearchpeer-review

    24 Citations (Scopus)


    The efficient and sustained immune response of an antigen requires T cell epitopes, capable of inducing a long lasting T cell memory. To detect T cell epitopes of the measles virus fusion protein (MV-F), the proliferation of lymphocytes from late convalescent donors in response to overlapping pentadecapeptides covering the whole protein sequence was studied. Three major immunodominant regions (F51-70, F121-135 and F211-225) containing promiscuous peptides induce proliferation in peripheral blood lymphocytes in ~ 50% of the donors. Potential DR1-restricted epitopes were mapped using an MHC competition binding assay. Both the proliferation and the binding data identified a DR1-restricted T cell epitope (F51-65). Contact sites of the peptide HQSLVIKLMPNITLL with MHC were characterized using substitution analogs. Alanine substitutions at most positions did not interfere with F51-65 binding. These analogs were therefore useful for studying the residues which were recognized by the TCR of MV- and F51-induced T cells lines. In addition to amino acid residues of the core of peptide F51-65 both the C-terminal and the N-terminal amino acids were essential for T cell interaction. Since peptides presented by class II molecules vary in length, these findings suggest that residues of the ragged tail are important for T cell activation. It is speculated that in late convalescent donors the length of the flanking sequence of MHC II-restricted peptides may play a role in controlling the heterogeneity of MV-specific T cell clones recruited as T helper/memory cells.

    Original languageEnglish
    Pages (from-to)445-456
    Number of pages12
    JournalInternational Immunology
    Issue number4
    Publication statusPublished - 1996


    • Antigen processing
    • DR1
    • Epitope
    • Peptide


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