Stimulation of Bordetella pertussis adenylate cyclase toxin intoxication by its hemolysin domain.
The internalization of the N-terminal catalytic domain of Bordetella pertussis adenylate cyclase toxin (ACT) across the cytoplasmic membrane has been considered to occur independently from protein-protein interactions which can lead to oligomerization required for hemolytic activity by its C-terminal hemolysin domain. Here we report that when added in excess, this hemolysin domain stimulates the internalization, suggesting the involvement of protein-protein interactions in cell-invasive activity of ACT, as well as its hemolytic activity.
Iwaki
M
M
Department of Bacterial and Blood Products, National Institute of Infectious Diseases, Musashimurayama-shi, Tokyo 208-0011, Japan. miwaki@nih.go.jp
Kamachi
K
K
Konda
T
T
D037361:Adenylate Cyclase Toxin; D001692:Biological Transport / Q000187:drug effects; D001886:Bordetella pertussis / Q000472:pathogenicity*; D004347:Drug Interactions; D006460:Hemolysin Proteins / Q000494:pharmacology*; D009154:Mutation; D010446:Peptide Fragments / Q000494:pharmacology*; D011485:Protein Binding; D010566:Virulence Factors, Bordetella / Q000235:genetics / Q000378:metabolism / Q000633:toxicity*
D037361:Adenylate Cyclase Toxin; D006460:Hemolysin Proteins; D010446:Peptide Fragments; D010566:Virulence Factors, Bordetella