Correlation between Shiga toxin B-subunit stability and antigen crosspresentation: a mutational analysis.
The homopentameric B-subunit of Shiga toxin (STxB) is used as a tool to deliver antigenic peptides and proteins to the cytosolic compartment of dendritic cells (DCs). In this study, a series of interface mutants of STxB has been constructed. All mutants retained their overall conformation, while a loss in thermal stability was observed. This effect was even more pronounced in trifluoroethanol solutions that mimic the membrane environment. Despite this, all mutants were equally efficient at delivering a model antigenic protein into the MHC class I-restricted antigen presentation pathway of mouse DCs, suggesting that the structural stability of STxB is not a key factor in the membrane translocation process.
Pina
David G
DG
Centre National de la Recherche Scientifique/UMR144, and Institut Curie, Centre de Recherche, Laboratoire Trafic, Signalisation et Ciblage Intracellulaires, Paris Cedex 05, France.
Stechmann
Bahne
B
Shnyrov
Valery L
VL
Cabanié
Lucien
L
Haicheur
Nacilla
N
Tartour
Eric
E
Johannes
Ludger
L
D000941:Antigens / Q000276:immunology*; D002942:Circular Dichroism; D005455:Fluorescent Antibody Technique; D006367:HeLa Cells; D006801:Humans; D008958:Models, Molecular; D009154:Mutation; D011487:Protein Conformation; D022603:Shiga Toxins / Q000737:chemistry* / Q000235:genetics / Q000276:immunology; D013056:Spectrophotometry, Ultraviolet
D000941:Antigens; D022603:Shiga Toxins