Characterization of human antibody to polyribophosphate, the capsular antigen of hemophilus influenzae, type B

作者: Richard B. Johnston , Porter Anderson , Fred S. Rosen , David H. Smith

DOI: 10.1016/0090-1229(73)90024-X

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摘要: Abstract The immunoglobulins involved in the human serologic response to polyribophosphate (PRP) 4 , capsular antigen of Hemophilus influenzae type b, have been studied. After immunization with 50 μg PRP, serum demonstrated primary antigen-binding capacity and a classic precipitin curve. Per unit weight, IgM from this was 100-fold more active than IgG PRP-specific hemagglutination 2-fold greater complement-dependent bactericidal activity. Specific anti-PRP antibody separated by immunoabsorption both assays; subgroups, only IgG1 detected preparation. high salt extract PRP precipitate hyperimmune serum, however, contained IgG2 ratio 1.6:1. Phagocytosis H. b vitro enhanced heated IgG, preparation but not IgM; activity approximately doubled addition complement. Inhibitor studies indicated that C 3 peptidase system.

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