Simultaneous Determination of Antibodies to Pertussis Toxin and Adenylate Cyclase Toxin Improves Serological Diagnosis of Pertussis

Regulation of pertussis toxin and lipopolysaccharide levels of Bordetella pertussis 134 in response to modulators

  Whooping cough (pertussis) is a highly contagious disease of the human respiratory tract, which is caused by Bordetella pertussis. Reemerge of pertussis in some highly immunized populations and divergency in gene order among several B. pertussis strains promoted this research to study the change of pertussis toxin (PT) and lipopolysacharide levels in response to the different environments. Th...

Suppression of platelet aggregation by Bordetella pertussis adenylate cyclase toxin.

The effect of Bordetella pertussis adenylate cyclase toxin (ACT) on platelet aggregation was investigated. This cell-invasive adenylate cyclase completely suppressed ADP (10 microM)-induced aggregation of rabbit platelets at 3 micrograms/ml and strongly suppressed thrombin (0. 2 U/ml)-induced aggregation at 10 micrograms/ml. The suppression was accompanied by marked increase in platelet intrace...

Bordetella pertussis Cyclase Toxin Promote Phagocytosis of Neutralizing Antibodies to Adenylate

Neutralizing antibodies to adenylate cyclase toxin promote phagocytosis of Bordetella pertussis by human neutrophils.

A previous study showed that opsonization with human immune serum could either promote or antagonize phagocytosis of Bordetella pertussis by human neutrophils depending on whether the bacteria expressed adenylate cyclase toxin. Opsonization of the wild-type strain inhibited phagocytosis relative to unopsonized controls. In contrast, mutants lacking adenylate cyclase toxin were efficiently phago...

Adenylate cyclase toxin-mediated delivery of the S1 subunit of pertussis toxin into mammalian cells.

The adenylate cyclase toxin (ACT) of Bordetella pertussis internalizes its catalytic domain into target cells. ACT can function as a tool for delivering foreign protein antigen moieties into immune effector cells to induce a cytotoxic T lymphocyte response. In this study, we replaced the catalytic domain of ACT with an enzymatically active protein moiety, the S1 (ADP-ribosyltransferase) subunit...