Immunomodulation of the antibody response to lipopolysaccharide in C3H/HeJ mice by complexing with heterologous ribosomes.
We show that formaldehyde fixation of Salmonella typhimurium lipopolysaccharide (LPS) to ribosomes purified from Brucella abortus induced a primary immunoglobulin M (IgM) response to LPS in C3H/HeJ mice and upon revaccination resulted in elevated titers of IgM and induction of IgG antibody to the O antigens of LPS, as measured by an enzyme-linked immunosorbent assay. A similar LPS-Aspergillus fumigatus ribosomal complex yielded IgM and IgG antibody to LPS only after secondary stimulation. These results demonstrate that the hyporesponsiveness of C3H/HeJ mice with respect to antibody formation to LPS can be overcome by complexing this molecule to ribosomal particles and provide a theoretical mechanism for the action of some "ribosomal" vaccines. The results are compatible with the hypothesis that LPS in complex with the ribosomes is converted to a T-dependent form of the antigen to which the C3H/HeJ mice can respond.
D000818:Animals; D000907:Antibodies, Bacterial / Q000032:analysis*; D000917:Antibody Formation; D005260:Female; D005557:Formaldehyde / Q000494:pharmacology; D007074:Immunoglobulin G / Q000032:analysis; D007075:Immunoglobulin M / Q000032:analysis; D008070:Lipopolysaccharides / Q000276:immunology*; D051379:Mice; D008809:Mice, Inbred C3H; D012270:Ribosomes / Q000276:immunology*; D012475:Salmonella / Q000276:immunology
D000907:Antibodies, Bacterial; D007074:Immunoglobulin G; D007075:Immunoglobulin M; D008070:Lipopolysaccharides; D005557:Formaldehyde