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

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 charac...

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Bibliographic Details
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
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Description
Summary: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.
ISSN:0264-410X
1873-2518
DOI:10.1016/S0264-410X(99)00210-8