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Updated: Aug 13, 2026

Peptide Scanning-assisted Identification of a Monoclonal Antibody-recognized Linear B-cell Epitope
Published on: March 24, 2017
Characterization of polyclonal antibodies raised against a linear peptide determinant of desmoglein-3
Giovanni Angelini1, Domenico Bonamonte, Mong-Shang Lin
1Department of Internal Medicine, Immunology and Infectious Diseases, Dermatology Section, Faculty of Medicine, University of Bari, P.za G. Cesare 11, 70124 Bari, Italy.
Our labs are pursueing the goal of exactly defining the qualities of peptide antigenicity, immunogenicity and pathogenicity in order to develop safe specific immunotherapies by utilizing specific portions of disease-associated-proteins (DAPs). Using as a model the Pemphigus vulgaris antigen (PVA) desmoglein 3 (Dsg3), we have studied the murine humoral response against the Dsg3 amino acid 49-60 peptide sequence, previously characterized as sequence having low similarity to the mouse proteome. The results show that the low-similarity Dsg3(49-60)REWVKFAKPCRE peptide does not elicit pathogenic antibodies.
Our labs are pursueing the goal of exactly defining the qualities of peptide antigenicity, immunogenicity and pathogenicity in order to develop safe specific immunotherapies by utilizing specific portions of disease-associated-proteins (DAPs). Using as a model the Pemphigus vulgaris antigen (PVA) desmoglein 3 (Dsg3), we have studied the murine humoral response against the Dsg3 amino acid 49-60 peptide sequence, previously characterized as sequence having low similarity to the mouse proteome. The results show that the low-similarity Dsg3(49-60)REWVKFAKPCRE peptide does not elicit pathogenic antibodies.
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