The binding of chimeric peptides to GM1 ganglioside enables induction of antibody responses after intranasal immunization

Abstract : 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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A. Delmas, Charalambos D Partidos. The binding of chimeric peptides to GM1 ganglioside enables induction of antibody responses after intranasal immunization. Vaccine, Elsevier, 1996, 14 (11), pp.1077-1082. ⟨10.1016/0264-410X(95)00239-W⟩. ⟨hal-02146915⟩

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