THE BINDING OF CHIMERIC PEPTIDES TO GM1 GANGLIOSIDE ENABLES INDUCTIONOF 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, t he 174-187 peptide from the G protein of the respiratory syncytial vir us, was co-linearly synthesized at the amino-(174-50) or carboxyl-term inus (50-174) of the 50-75 peptide. Although both chimeric peptides we re equally immunogenic by the intraperitoneal route, the 50-174 peptid e 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 effec tive inhibitor than the 174-50 peptide. In addition, an effective prim ing of the immune system was achieved after the i.n. administration of immunogens. The observed unresponsiveness after the i.n. co-immunizat ion with the 50-174 peptide and GM1 ganglioside emphasize the role of GM1 binding for the induction of an immune response after i.n. immuniz ation. Copyright (C) 1996 Elsevier Science Ltd.