ABSTRACT
A soluble fraction obtained from Bordetella pertussis was evaluated as adjuvant for the pertussis component of the Diphtheria-Pertussis-Tetanus (DPT) vaccine. High levels of antibodies were induced, and a 78% protection rate of mice challenged with live B. pertussis was observed. Two proteins were identified as the 73 kDa N-terminal alpha-domain of BrkA autotransporter protein and the Cpn60/60 kDa chaperonin. Both stimulated antibodies against pertussis and induced a 42% protection rate against the challenge. IgG1 and IgG2a were stimulated suggesting that the immune response could be modulated to produce Th1 or Th2.
Subject(s)
Bacterial Outer Membrane Proteins/immunology , Bordetella pertussis/immunology , Chaperonin 60/immunology , Pertussis Vaccine/immunology , Whooping Cough/immunology , Adjuvants, Immunologic , Amino Acid Sequence , Animals , Bacterial Outer Membrane Proteins/chemistry , Female , Mice , Mice, Inbred BALB C , Molecular Sequence Data , Protein Structure, Tertiary , Whooping Cough/microbiologyABSTRACT
A soluble fraction obtained from Bordetella pertussis was evaluated as adjuvant for the pertussis component of the Diphtheria-Pertussis-Tetanus (DPT) vaccine. High levels of antibodies were induced, and a 78% protection rate of mice challenged with live B. pertussis was observed. Two proteins were identified as the 73 kDa N-terminal á-domain of BrkA autotransporter protein and the Cpn60/60 kDa chaperonin. Both stimulated antibodies against pertussis and induced a 42% protection rate against the challenge. IgG1 and IgG2a were stimulated suggesting that the immune response could be modulated to produce Th1 or Th2.
