Stimulation of Bordetella pertussis adenylate cyclase toxin intoxication by its hemolysin domain

Infect Immun. 2000 Jun;68(6):3727-30. doi: 10.1128/IAI.68.6.3727-3730.2000.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenylate Cyclase Toxin*
  • Biological Transport / drug effects
  • Bordetella pertussis / pathogenicity*
  • Drug Interactions
  • Hemolysin Proteins / pharmacology*
  • Mutation
  • Peptide Fragments / pharmacology*
  • Protein Binding
  • Virulence Factors, Bordetella / genetics
  • Virulence Factors, Bordetella / metabolism
  • Virulence Factors, Bordetella / toxicity*

Substances

  • Adenylate Cyclase Toxin
  • Hemolysin Proteins
  • Peptide Fragments
  • Virulence Factors, Bordetella