Increasing the potency of MHC class II-presented epitopes by linkage to Ii-Key peptide

• Published in: Vaccine 2000-06, Vol.18 (24), p.2693-2697
• Main Authors: Humphreys, R.E., Adams, S., Koldzic, G., Nedelescu, B., von Hofe, E., Xu, M.
• Format: Article
• Language: English
• Subjects: AIi protein; Amino Acid Sequence; Animals; Antigens; Antigens, CD - immunology; Antigens, Differentiation, B-Lymphocyte - immunology; Binding Sites; Biological and medical sciences; Cell Line; Cytochrome c Group - immunology; Fundamental and applied biological sciences. Psychology; Fundamental immunology; Histocompatibility antigens (hla, h-2 and other systems); Histocompatibility Antigens Class II - immunology; Hybrids; Ii-key peptide; MHC class II; Molecular immunology; Molecular Sequence Data; Peptide vaccines; Protein Structure, Secondary
• ISSN: 0264-410X; 1873-2518
• DOI: 10.1016/S0264-410X(00)00067-0

We previously found that peptide Ii77-92 from the immunoregulatory Ii protein significantly enhances the binding of antigenic peptides to MHC class II molecules. Now a series of hybrids have been constructed linking LRMK, the active core region of the Ii77-92 peptide, to an antigenic epitope of cytochrome C. In vitro T cell hybridoma stimulation by some of these hybrids is up to 250 times more potent than by the antigenic peptide. The biological activities of the hybrids were tested in terms of length and composition of the linker. Simple spacers containing a polymethylene bridge (-HN-CH 2-CH 2-CH 2-CH 2-CO 2-) were fully active in these hybrids which can enhance vaccination with MHC class II-presented epitopes.