RESUMO
A GroEL-like protein from Bordetella pertussis was purified. This protein was found to have the tetradecameric subunit structure typical of the GroEL family of proteins and to contain epitopes similar to those of other members of this family, including a human GroEL-like protein. Active immunization of neonatal mice with the B. pertussis GroEL-like protein provided little protection against an aerosol challenge with B. pertussis. Antibodies to this protein were elicited in mice by a standard diphtheria-tetanus-pertussis (DTP) vaccine but not by an experimental acellular pertussis vaccine. Since the Bordetella GroEL-like protein was found to contain epitopes similar to those on the mammalian analog, the potential exists that vaccination with standard DTP vaccines may induce antibodies which react with the mammalian GroEL analog.
Assuntos
Proteínas de Bactérias/isolamento & purificação , Bordetella pertussis/análise , Animais , Artrite Reumatoide/imunologia , Proteínas de Bactérias/imunologia , Vacina contra Difteria, Tétano e Coqueluche/imunologia , Humanos , Camundongos , Camundongos Endogâmicos BALB C , Peso Molecular , VacinaçãoRESUMO
A purification scheme was devised for a 69-kDa outer membrane protein of Bordetella pertussis, a virulence-associated protein which may play a role in the pathogenesis of the organism. The protein was purified to apparent homogeneity by heating B. pertussis cells for 1 h at 60 degrees C followed by DEAE-Sepharose and Affi-Gel Blue chromatography. Antibodies found in sera obtained from patients diagnosed as having pertussis reacted with this protein. This purification scheme should be useful for the production of the 69 kDa protein which is currently being evaluated as a pertussis vaccine candidate.
