Lysenin

<p>Lysenin is a <a href="/facts/Pore-forming_toxin/MEj5bHdt">pore-forming toxin</a> (PFT) present in the <a href="/facts/Coelom/PD25dd6m">coelomic</a> fluid of the <a href="/facts/Earthworm/V7IUvWgQ">earthworm</a> <i><a href="/facts/Eisenia_fetida/YTTptudz">Eisenia fetida</a></i>. Pore-forming toxins are a group of <a href="/facts/Protein/Jxmagu3E">proteins</a> that act as virulence factors of several <a href="/facts/Pathogen/axMXtV1M">pathogenic</a> <a href="/facts/Bacteria/wC8xSCsU">bacteria</a>. Lysenin proteins are chiefly involved in the defense against cellular pathogens. Following the general mechanism of action of PFTs lysenin is segregated as a soluble monomer that binds specifically to a <a href="/facts/Membrane_receptor/0YGSjDdL">membrane receptor</a>, <a href="/facts/Sphingomyelin/KruAelVs">sphingomyelin</a> in the case of lysenin. After attaching to the membrane, the oligomerization begins, resulting in a nonamer on top of membrane, known as a prepore. After a conformational change, which could be triggered by a decrease of <a href="/facts/PH/RnSv8D7y">pH</a>, the oligomer is inserted into the membrane in the so-called pore state.
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Lysenin open-in-new

Lysenin