Sandbox Reserved 1237: Difference between revisions

No work has yet been done on specific Slx-2 binding to Gb3, but it can be assumed due to the homology present between the two, as well as their shared receptor, that the mechanisms are roughly the same. The binding of the B subunit to G3b occurs at one to three receptor sites on the subunits, the third of which is has a lower affinity than the first two. As the B subunits bind with high affinity, the cluster of verotoxin expands laterally across the membrane, causing it to invaginate with or without the assistance of cellular tubules such as actin or dynamin. Such invagination give way to the formation of vesicles which transport the toxins into the cell. Once there, the A subunit is cleaved by the action of furin to form A1 and A2. A2 keeps A1 bound to the B pentamer, while A1 carries out the endohydrolysis of the N-glycosidic bond at a specific adenosine on the 28S rRNA unit of a 60S ribosome. This halts protein synthesis, killing the cell. With Stx, the dead cells release cytokines and chemokines, which play a role in platelet activation. Stx also inactivates ADAMTS13, which is involved in cleaving a protein that is involved in blood clotting, thus increasing the level of platelet activation further, eventually leading to the formation of microthrombi. [3],[4],[5],[6].

== Disease ==