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Binding immune-stimulating oligonucleotides to cationic peptides from viral core antigen enhances their potency as
Petra Riedl1, Michael Buschle, Jörg Reimann
1Institute for Medical Microbiology and Immunology, University of Ulm, Ulm, Germany.
Abstract:
Priming specific Th1 immunity by recombinant hepatitis B core antigen (HBcAg) depends on its arginine (Arg)-rich, 34-36-residue-long C terminus, and nucleotides bound to it. This adjuvant activity intrinsic to HBcAg facilitates priming of Th1 immunity to co-delivered, unrelated antigens, such as hepatitis B surface antigen (HBsAg), or ovalbumin (OVA) that prime specific Th2 immunity when injected without adjuvants. We loaded immune-stimulating, CpG-containing oligodeoxynucleotides (ODN) to the HBcAg-derived Arg-rich peptides C-1 (HBcAg(150-157), RRRDRGRS) or C-2 (HBcAg(164-179), SPRRRRSQSPRRRRSQ). When these peptide/nucleotide complexes were co-injected into mice with HBsAg, hepatitis B precore antigen (HBeAg) or OVA, the animals developed strikingly higher serum IgG2 antibody titers and cytotoxic T lymphocyte responses than animals co-injected with these antigens and 'free' (not peptide-bound) ODN. Potent Th1-promoting adjuvants can thus be synthesized that mimic priming of anti-viral immunity by natural nucleocapsid particles.