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- W2000995217 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." @default.
- W2000995217 created "2016-06-24" @default.
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- W2000995217 date "2002-06-01" @default.
- W2000995217 modified "2023-10-02" @default.
- W2000995217 title "Binding immune-stimulating oligonucleotides to cationic peptides from viral core antigen enhances their potency as adjuvants" @default.
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- W2000995217 doi "https://doi.org/10.1002/1521-4141(200206)32:6<1709::aid-immu1709>3.0.co;2-d" @default.
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