Abstract
Viruses are intracellular parasites which utilize their host cell's subcellular machinery for their own replication by remodeling of the host's intracellular membranes. Lipids with phosphatidylinositol-4-phosphate (PI4P) head groups have been found to be crucial for the formation of these replication organelles in enteroviruses and flaviviruses. Lipid binding assays show that poliovirus protease 3Cpro specifically binds to PI4P. Using NMR spectroscopy, binding with other phosphatidylinositol phosphates (PIPs) has been detected and specific residues has been identified which exhibits chemical shift changes upon binding with 3Cpro. PI3P, PI4P, and PI5P have been found to exhibit similar chemical shift perturbation patterns upon binding with 3Cpro. Our results indicate that a novel PIP binding site has been identified, with some residues exhibiting long range interactions (or a secondary binding site).
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