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The B-subunits of cholera and Shiga toxins are functionally and structurally related proteins with different chain lengths and no sequence similarity. They are responsible for toxin binding to specific glycosphingolipid receptors and intracellular toxin trafficking. Indeed, it is clearly established that B-subunits have the unique capacity of targeting the toxins to a poorly explored intracellular pathway, the retrograde route, allowing the transfer to the cytosol of the associated catalytic A-subunits, by retro-translocation from the endoplasmic reticulum. The B-subunits have also been used as vectors for antigen presentation in immunotherapeutic approaches. It is, however, not known if and how the B-subunits intervene in membrane translocation of the A-subunits and/or antigens to the cytosol. Therefore, it is important to characterise the driving force of pentamer formation, its conformational stability, and toxin–receptor …