Molecular parameters in melittin immunogenicity

• Published in: Journal of peptide science Vol. 3; no. 4; pp. 267 - 276
• Main Authors: Curicio-Vonlanthen, Véronique, Schneider, Conrad H., Frutig, Karin, Blaser, Kurt, Kalabacher, Hubert
• Format: Journal Article
• Language: English
• Published: Chichester, UK John Wiley & Sons, Ltd 01.07.1997
• Subjects: Amino Acid Sequence; Animals; Cell Division - immunology; Cell Line; Clone Cells; Epitopes, T-Lymphocyte - immunology; Guinea Pigs; human T-cell clone; Humans; Melitten - chemistry; Melitten - immunology; melittin immunogenicity; Mice; Mice, Inbred BALB C; Molecular Sequence Data; substituents on melittin; T-cell epitopes; T-Lymphocytes - cytology; T-Lymphocytes - immunology; truncated melittin
• ISSN: 1075-2617; 1099-1387
• DOI: 10.1002/(SICI)1099-1387(199707)3:4<267::AID-PSC106>3.0.CO;2-7

Based on immunogenicity studies, two T‐cell epitopes in melittin were found to be functional in guinea pigs, one being centrally located, the other one residing in the C‐terminal chain. In Balb/c mice only the central epitope was found to be active. A human T‐cell clone was found by T‐cell proliferation studies to employ strictly the C‐terminal chain. Truncation of melittin peptides at the N‐terminus did not markedly affect the capacity of guinea pigs to develop anti‐IgG responses towards peptidic epitopes and towards a C‐terminally attached haptenic group. Attachment of various substituents inside and outside the T‐cell epitopic areas had no marked effect on antibody responses. In contrast, the substituents positioned within a T‐cell epitope abolished T‐cell proliferation. This difference between whole animal data and cellular in vitro responses is presently not understood. © 1997 European Peptide Society and John Wiley & Sons, Ltd.