Structural features of a chimeric peptide inducing cytotoxic T lymphocyte responses in saline.

Abstract : Little information is available correlating the structural properties of peptides with their immunogenicity in terms of responses via cytotoxic T lymphocytes (CTLs). The TT-NP6 chimeric peptide, consisting of two copies of a promiscuous T-helper epitope (T: residues 288-302 from the fusion protein of the measles virus) linked to the NP6 T-cytotoxic epitope (NP6: residues 52-60 from the nucleoprotein of measles virus) was able to induce virus-specific CTL responses in the absence of any adjuvant and hydrophobic component. The present work was undertaken to gain insight into structural features of the TT-NP6 peptide that may be important in optimizing the CTL immunogenicity of the peptide. Circular dichroism data, obtained in a buffer of physiological ionic strength and pH, strongly suggest a self-associated state for the peptide, which was confirmed by a sedimentation velocity experiment. However, helix association is accompanied by loss of overall helical content. Thermal-dependence studies show that the unfolding of self-associated alpha-helices is significantly more pronounced than the unfolding of isolated alpha-helices. Circular dichroism data, together with tryptic limited proteolysis, suggest the presence of a charged amino acid within the hydrophobic core. This study should provide a basis for engineering more effective immunogenic peptides against the measles virus by increasing the stability of the TT-NP6 peptide.
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Submitted on : Tuesday, June 4, 2019 - 11:16:39 AM
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  • HAL Id : hal-02146737, version 1
  • PUBMED : 10491190



C Delmotte, E Le Guern, Y. Trudelle, A. Delmas. Structural features of a chimeric peptide inducing cytotoxic T lymphocyte responses in saline.. European Journal of Biochemistry, Wiley, 1999, 265 (1), pp.336-45. ⟨hal-02146737⟩



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