Enhancement of peptide immunogenicity by linear polymerization

Eur J Immunol. 1988 Feb;18(2):199-202. doi: 10.1002/eji.1830180203.

Abstract

The effect of linear homopolymerization on the immunogenicity of synthetic peptides was studied using either haptenic peptides (representing amino acid sequences 103-115 and 133-147 of bovine rotavirus major protein) or immunogenic peptides TD-103-115 and TD-133-147 which were constructed by co-linear synthesis of the former peptides and an amino acid sequence representing a determinant recognized by T helper cells (TD). It was found that the two haptenic peptides were rendered immunogenic by linear homopolymerization. Moreover, homopolymerization also enhanced the immunogenicity of TD-103-115 but not that of TD-133-147. In the three cases where polymerization enhanced immunogenicity, a reinforced amphipathic pattern was predicted in the neighborhood of the junction of the monomers. The possibility that polymerization might have generated a new T cell determinant is discussed.

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Antibody Formation*
  • Antigens, Viral / administration & dosage
  • Antigens, Viral / immunology
  • Epitopes / analysis
  • Epitopes / immunology*
  • Female
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral / analysis
  • Hemagglutinins, Viral / immunology
  • Macromolecular Substances
  • Mice
  • Mice, Inbred BALB C
  • Molecular Sequence Data
  • Peptide Fragments / administration & dosage
  • Peptide Fragments / immunology*
  • Serum Albumin, Bovine / administration & dosage
  • Serum Albumin, Bovine / analysis
  • Serum Albumin, Bovine / immunology
  • T-Lymphocytes, Helper-Inducer / immunology

Substances

  • Antigens, Viral
  • Epitopes
  • Hemagglutinin Glycoproteins, Influenza Virus
  • Hemagglutinins, Viral
  • Macromolecular Substances
  • Peptide Fragments
  • Serum Albumin, Bovine