Nonepitopic antibody binding sequence: implications in screening and development of peptide vaccines

• Published in: Vaccine 1999-09, Vol.18 (3), p.315-320
• Main Authors: Adesida, Adetola B, Aojula, Raj R, Aojula, Harmesh S, Clarke, David J
• Format: Article
• Language: English
• Subjects: Antigen-Antibody Reactions; Applied microbiology; Biological and medical sciences; Enzyme-Linked Immunosorbent Assay; Epitopes; Fundamental and applied biological sciences. Psychology; Microbiology; multiple antigen peptide; Nonepitopic sequences; Peptide Library; Peptide vaccines; Polyclonal IgGs; Protein Binding; Sequence Analysis, Protein; Vaccines, antisera, therapeutical immunoglobulins and monoclonal antibodies (general aspects); Vaccines, Synthetic
• ISSN: 0264-410X; 1873-2518
• DOI: 10.1016/S0264-410X(99)00210-8

We describe the interaction of a nonepitopic synthetic decapeptide sequence comprising, GQVLQGAIKG, derived from a random sequence with polyclonal IgGs from various animal sources. GQVLQGAIKG was screened for antibody binding activity using ELISA techniques. The peptide showed similar binding characteristics to the IgGs tested. The results were similar whether we used peptide acid or amide. MAP (multiple antigen peptide)-type construct of the peptide was synthesised and employed as an approach to enhance peptide-IgG interaction. The construct, (GQVLQGAIKG) 4-K 2-K, showed significant antibody binding activity relative to its monomeric form. These results show that nonepitopic sequences may contribute to binding activity observed in peptide library screening and development of peptide based vaccines. As a cautionary point the measure of antibody binding cannot alone be used to classify peptide as an antigen.