Aggregation and fusion of lipid vesicles induced by diphtheria toxin at low pH: possible involvement of the P site and the NAD+ binding site.
Model membranes have been used to study the interaction between diphtheria toxin and lipids. We report here on the ability of this toxin to induce, at low pH, fusion and aggregation of asolectin lipid vesicles. Resonance energy transfer experiments using lipid fluorescent probes make it possible to discriminate between these two processes.
D000255:Adenosine Triphosphate / Q000378:metabolism; D001665:Binding Sites; D004167:Diphtheria Toxin / Q000378:metabolism / Q000494:pharmacology*; D005456:Fluorescent Dyes; D006863:Hydrogen-Ion Concentration; D008081:Liposomes; D008561:Membrane Fusion / Q000187:drug effects*; D009243:NAD / Q000378:metabolism; D009391:Nephelometry and Turbidimetry; D010446:Peptide Fragments / Q000378:metabolism; D010713:Phosphatidylcholines; D010743:Phospholipids; D013050:Spectrometry, Fluorescence
D004167:Diphtheria Toxin; D005456:Fluorescent Dyes; D008081:Liposomes; D010446:Peptide Fragments; D010713:Phosphatidylcholines; D010743:Phospholipids; C029795:diphtheria toxin fragment A; C039171:diphtheria toxin fragment B; D009243:NAD; C024990:asolectin; D000255:Adenosine Triphosphate