Enhancement of peptide immunogenicity by insertion of a cathepsin B cleavage site between determinants recognized by B and T cells.
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.
Sarobe
P
P
Departamento de Medicina Interna, Universidad de Navarra, Facultad de Medicina, Pamplona, Spain.
Lasarte
J J
JJ
Larrea
E
E
Golvano
J J
JJ
Prieto
I
I
Gullón
A
A
Prieto
J
J
Borrás-Cuesta
F
F
D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation; D000938:Antigen-Presenting Cells / Q000502:physiology; D001402:B-Lymphocytes / Q000276:immunology*; D002401:Cathepsin B / Q000494:pharmacology*; D000939:Epitopes; D005260:Female; D051379:Mice; D008807:Mice, Inbred BALB C; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000276:immunology*; D013601:T-Lymphocytes / Q000276:immunology*
D000939:Epitopes; D010446:Peptide Fragments; D002401:Cathepsin B