Correlation between Shiga toxin B-subunit stability and antigen crosspresentation: a mutational analysis |
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Authors: | Pina David G Stechmann Bahne Shnyrov Valery L Cabanié Lucien Haicheur Nacilla Tartour Eric Johannes Ludger |
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Affiliation: | Centre National de la Recherche Scientifique/UMR144, and Institut Curie, Centre de Recherche, Laboratoire Trafic, Signalisation et Ciblage Intracellulaires, Paris Cedex 05, France. |
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Abstract: | 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. |
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Keywords: | STxB, Shiga toxin B-subunit CD, circular dichroism DC, dendritic cell ER, endoplasmic reticulum TFE, trifluoroethanol |
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