Enhancement of peptide immunogenicity by insertion of a cathepsin B cleavage site between determinants recognized by B and T cells
Sarobe P, Lasarte JJ, Larrea E, Golvano JJ, Prieto I, Gullón A, Prieto J, Borrás-Cuesta F.
Departamento de Medicina Interna, Universidad de Navarra, Facultad de Medicina, Pamplona, Spain.
Magazine: Research in Immunolog
Date: May 1, 1993Hepatology
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 ir 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.
CITATION Res Immunol. 1993 May;144(4):257-62
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