Secondary structure of anthrax lethal toxin proteins and their interaction with large unilamellar vesicles: a fourier-transform infrared spectroscopy approach.
Attenuated total reflection Fourier transform infrared spectroscopy has been used to study the secondary structure of anthrax lethal toxin proteins: protective antigen (PA) and lethal factor (LF), as a function of pH in the absence and in the presence of phospholipid vesicles. We first characterized the binding of LF and PA to the lipid membrane and demonstrated the strong pH dependence of the association of PA and LF to the lipid bilayer as well as the effect of pH neutralization on this binding. Binding of LF to the lipid membrane can be, at least partially, reversed when the pH is brought to neutral whereas in the same conditions PA binding is irreversible. Characterization of the conformational changes undergone by PA and LF upon pH lowering, lipid binding, and, in the case of LF, reversal of binding was carried out (i) by determining the secondary structure of the proteins and (ii) by evaluating their ability to undergo an hydrogen/deuterium exchange.
Wang
X M
XM
Laboratoire de Chimie Physique des Macromolécules aux Interfaces, Université Libre de Bruxelles, Belgium.
Mock
M
M
Ruysschaert
J M
JM
Cabiaux
V
V
D000942:Antigens, Bacterial; D001408:Bacillus anthracis; D001427:Bacterial Toxins / Q000737:chemistry* / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D050356:Lipid Metabolism; D008081:Liposomes; D017433:Protein Structure, Secondary; D017550:Spectroscopy, Fourier Transform Infrared
D000942:Antigens, Bacterial; D001427:Bacterial Toxins; D008081:Liposomes; C030325:anthrax toxin