The binding of chimeric peptides to GM1 ganglioside enables induction of antibody responses after intranasal immunization.
With a model peptide, the neutralizing epitope 50-75 of cholera toxin B subunit, two chimeric peptides were constructed. A T-cell epitope, the 174-187 peptide from the G protein of the respiratory syncytial virus, was co-linearly synthesized at the amino-(174-50) or carboxyl-terminus (50-174) of the 50-75 peptide. Although both chimeric peptides were equally immunogenic by the intraperitoneal route, the 50-174 peptide was more immunogenic than the 174-50 peptide by the intranasal (i.n.) route. Both chimeric peptides inhibited the binding of cholera toxin B subunit to GM1 ganglioside with the 50-174 peptide being more effective inhibitor than the 174-50 peptide. In addition, an effective priming of the immune system was achieved after the i.n. administration of immunogens. The observed unresponsiveness after the i.n. co-immunization with the 50-174 peptide and GM1 ganglioside emphasize the role of GM1 binding for the induction of an immune response after i.n. immunization.
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Department of Clinical Sciences, London School of Hygiene and Tropical Medicine, UK.
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D000281:Administration, Intranasal; D000595:Amino Acid Sequence; D000818:Animals; D000917:Antibody Formation / Q000276:immunology*; D005260:Female; D005677:G(M1) Ganglioside / Q000008:administration & dosage / Q000276:immunology*; D051379:Mice; D008810:Mice, Inbred C57BL; D008969:Molecular Sequence Data; D010455:Peptides / Q000008:administration & dosage / Q000276:immunology; D011485:Protein Binding / Q000276:immunology; D011993:Recombinant Fusion Proteins / Q000008:administration & dosage / Q000276:immunology*
D010455:Peptides; D011993:Recombinant Fusion Proteins; D005677:G(M1) Ganglioside