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Characterization of polyclonal antibodies raised against a linear peptide determinant of desmoglein-3

  • Giovanni Angelini
  • , Domenico Bonamonte
  • , Mong Shang Lin
  • , Alberta Lucchese
  • , Abraham Mittelman
  • , Rosario Serpico
  • , Simone Simone
  • , Animesh A. Sinha
  • , Darja Kanduc
  • University of Bari
  • Medical College of Wisconsin
  • New York Medical College

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

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 Dsg349-60REWVKFAKPCRE peptide does not elicit pathogenic antibodies.

Original languageEnglish
Pages (from-to)1-7
Number of pages7
JournalJournal of Experimental Therapeutics and Oncology
Volume5
Issue number1
StatePublished - 2005

Keywords

  • Desmoglein 3
  • Low-similarity sequence
  • Pemphigus vulgaris
  • Peptide Immunotherapy
  • Proteomics

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