Shiga toxins are a family of related toxins with two major groups, Stx1 and Stx2, expressed by genes considered to be part of the genome of lambdoid prophages. The toxins are named for Kiyoshi Shiga, who first described the bacterial origin of dysentery caused by Shigella dysenteriae.
As the name suggests, this little bugger causes pretty bad dysentery in humans. Shiga-like Toxin is made of 6 primary chains, 5 smaller identical subunits that form a pentamer ring and then the Alpha unit. The two red domains on top are the functionally toxic portions of the protein.
The pentamer is the portion of the compound that binds to surface receptors anchoring the Alpha unit toxin to the membrane. Upon binding, the Alpha unit forces itself into the cytosol. Following this, a predict bile sequence of events occurs that directly inactivates ribosomes halting protein synthesis.
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