Contribution of the B oligomer to the protective activity of genetically attenuated pertussis toxin.
An enzymatically deficient recombinant S1 subunit, in which Arg-9 was replaced by Lys, was combined with native B oligomer to form a mutant holotoxin molecule. This molecule exhibited decreased leukocytosis-promoting and histamine-sensitizing activities compared with those of the native toxin, supporting the view that the B oligomer is not responsible for these activities. The protective activity of this genetically attenuated pertussis toxin was compared with that of B oligomer alone. The mutant pertussis toxin and B oligomer were similarly capable of protecting mice against a respiratory infection with Bordetella pertussis, suggesting that the B oligomer makes a significant contribution to the protection afforded by the genetically attenuated holotoxin.
Arciniega
J L
JL
Division of Bacterial Products, Center for Biologics Evaluation and Research, Bethesda, Maryland 20892.
Shahin
R D
RD
Burnette
W N
WN
Bartley
T D
TD
Whiteley
D W
DW
Mar
V L
VL
Burns
D L
DL
D000818:Animals; D000907:Antibodies, Bacterial / Q000032:analysis; D006224:Cricetinae; D005260:Female; D007114:Immunization; D051379:Mice; D008807:Mice, Inbred BALB C; D037342:Pertussis Toxin; D010567:Pertussis Vaccine / Q000276:immunology*; D014613:Vaccines, Attenuated / Q000276:immunology; D014614:Vaccines, Synthetic / Q000276:immunology*; D010566:Virulence Factors, Bordetella / Q000276:immunology*
D000907:Antibodies, Bacterial; D010567:Pertussis Vaccine; D014613:Vaccines, Attenuated; D014614:Vaccines, Synthetic; D010566:Virulence Factors, Bordetella; D037342:Pertussis Toxin