Structural and functional relationships between HCV NS5A and NS5B and the human Cyclophilins


To replicate the Hepatitis C Virus (HCV) requires, in addition to its own proteins, the intervention of host cell factors. Among these cell factors the human Cyclophilin A (CypA) protein with its enzymatic peptidyl prolyl cis-trans isomerase (PPIase) activity is mandatory for efficient HCV replication and production of nouvel infectious particles. We are focusing on the deciphering of the structural and functional aspects resulting from the interaction between the human CypA and two HCV proteins: NS5A, a multifunctional protein for which no precise molecular activity has been identified, and NS5B, the viral RNA-dependent RNA polymerase. Our main investigation tool is the Nuclear Magnetic Resonance (NMR) spectroscopy that indeed enables us to study the structural ans functional aspects of the problem as well

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HCV and Cyp