Understanding the role of cholesterol in pore forming pathway of CytolysinA through atomistic Molecular Dynamics.
Cholesterol has been known to act as a receptor for many Pore forming proteins(PFPs). A major subclass of PFPs are the hostile proteins known as Pore forming Toxins (PFTs). PFTs punch holes in the cell membrane causing cell lysis due to ion imbalance. These proteins are secreted as water-soluble monomer form but upon encounter of the membrane, they undergo significant conformational changes to form an oligomeric pore.The PFT we are interested is a α-hemolysin secreted by bacteria called Cytolysin A (ClyA). The structure of ClyA has been resolved in both of its forms: 1) water-soluble and 2) transmembrane oligomerized pore. Availability of the structures makes ClyA ideal for studying α-PFTs for simulation. We are looking into how cholesterol interacts with ClyA.