Structural Properties of Chimeric Peptides Containing a T‐cell Epitope Linked to a Fusion Peptide and their Importance for in Vivo Induction of Cytotoxic T‐cell Responses

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Abstract
We have previously shown that when administered to mice without adjuvant, a chimeric peptide consisting of the fusion peptide F from measles virus protein linked at the C‐terminus of a cytotoxic T‐cell epitope from the M2 protein of respiratory syncytial virus efficiently primes for an major histocompatibility complex (MHC) class‐I restricted cytotoxic T lymphocyte (CTL) response. In this report, we demonstrated by microspectrofluorometry that the fusion‐peptide moiety bound to the plasma membrane of living cells. When the fusion peptide was linked to the C‐terminus of the CTL epitope, the chimeric peptide (M2–F) adopted a marked β‐sheet conformation. In contrast, when the fusion peptide was linked to the N‐terminus of the T‐cell epitope (F–M2), the chimeric peptide adopted an a‐helical conformation in the presence of trifluoroethanol. The immunogenicity of the two chimeric peptides for class‐I restricted CTL was also significantly different, the one adopting the a‐helical conformation being more immunogenic. Probably due to its obvious conversion to an α‐helical conformation, the F–M2 peptide could have a higher propensity to insert into membranes, as shown by microspectrofluorometry, with a resultant better immunogenicity than the M2–F peptide.

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