Diphtheria toxin and its mutant crm 197 differ in their interaction with lipids.
The interaction of diphtheria toxin and its enzymatically deficient mutants crm 176 and crm 197 with liposomes has been studied by turbidity measurement and hydrophobic photolabelling with photoactivatable phosphatidylcholines. Diphtheria toxin and crm 176 at neutral pH bind to the surface of lipid bilayers while crm 197 also appears to interact with the fatty acid chains of phospholipids. All proteins undergo a change in conformation over the same range of acidic pH and become able to insert in the lipid bilayer. The tighter lipid interaction of crm 197 may account for its higher cell association constant. The possibility is discussed that the binding of diphtheria toxin to cells is mediated by both a protein receptor and an interaction with the head group of phospholipids.
D004167:Diphtheria Toxin / Q000235:genetics* / Q000378:metabolism; D066257:Heparin-binding EGF-like Growth Factor; D006863:Hydrogen-Ion Concentration; D036341:Intercellular Signaling Peptides and Proteins; D050356:Lipid Metabolism; D008081:Liposomes; D009391:Nephelometry and Turbidimetry; D010743:Phospholipids / Q000378:metabolism; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic / Q000378:metabolism*
D004167:Diphtheria Toxin; D066257:Heparin-binding EGF-like Growth Factor; D036341:Intercellular Signaling Peptides and Proteins; D008081:Liposomes; D010743:Phospholipids; D011956:Receptors, Cell Surface; D011950:Receptors, Cholinergic