Internal lysine palmitoylation in adenylate cyclase toxin from Bordetella pertussis

Science. 1994 Oct 21;266(5184):433-5. doi: 10.1126/science.7939682.


A number of bacterial protein toxins, including adenylate cyclase (AC) toxin from Bordetella pertussis, require the product of an accessory gene in order to express their biological activities. In this study, mass spectrometry was used to demonstrate that activated, wild-type AC toxin was modified by amide-linked palmitoylation on the epsilon-amino group of lysine 983. This modification was absent from a mutant in which the accessory gene had been disrupted. A synthetic palmitoylated peptide corresponding to the tryptic fragment (glutamine 972 to arginine 984) that contained the acylation blocked AC toxin-induced accumulation of adenosine 3',5'-monophosphate, whereas the non-acylated peptide had no effect.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Acylation
  • Adenylate Cyclase Toxin*
  • Amino Acid Sequence
  • Animals
  • Chromatography, High Pressure Liquid
  • Cyclic AMP / metabolism
  • Hemolysis
  • Humans
  • Lysine / metabolism*
  • Mass Spectrometry
  • Molecular Sequence Data
  • Mutation
  • Palmitates / metabolism*
  • Peptide Fragments / chemistry
  • Peptide Fragments / toxicity
  • Sheep
  • Tumor Cells, Cultured
  • Virulence Factors, Bordetella / chemistry
  • Virulence Factors, Bordetella / metabolism*
  • Virulence Factors, Bordetella / toxicity


  • Adenylate Cyclase Toxin
  • Palmitates
  • Peptide Fragments
  • Virulence Factors, Bordetella
  • Cyclic AMP
  • Lysine