Immunogenicity Peptide Lysine B cell T cell IL2 Determinant Cathepsin B Antigen processing
Sarobe P, Lasarte JJ, Larrea E, Golvano JJ, Prieto I, Gullon A, et al. Enhancement of peptide immunogenicity by insertion of a cathepsin B cleavage site between determinants recognized by B and T cells. Res Immunol 1993 May;144(4):257-262.
The insertion of two lysine residues (cleavage sites of cathepsin B) at the boundary of a peptide recognized by B cells (BD) and a class-II- presentable sequence (TDh) enhanced the anti-BD antibody induction capacity of this type of peptide construct, as well as production of IL2. It is postulated that these lysines generate a neoprocessable site which helps in release of the TDh moiety from the construct, enabling its presentation to class II molecules, an essential step in clonal expansion of the antibody-producing B cell after internalization of the construct via the BD moiety.