Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2050661 | FEBS Letters | 2008 | 5 Pages |
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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Authors
David G. Pina, Bahne Stechmann, Valery L. Shnyrov, Lucien CabaniƩ, Nacilla Haicheur, Eric Tartour, Ludger Johannes,