(p58). A higher rate of p58 seems to induce HCV assembly, whereas a lack of p58 leads to RNA replication. But the actual role of phosphorylation of NS5A is not clear. However, NS5A does not only regulate HCV replication and assembly, it also inhibits apoptosis, so the infected cell cannot disintegrate by itself and contain the infection, as cells normally do. Because of the lack of apoptosis, mutations within the cellular genome also do not trigger cells death. This causes the promotion of tumours. Mechanism of action NS5A contains a binding pocket in domain 1, where daclatasvir can insert. Because of the symmetric and amino acid related structure of daclatasvir, it comes to H-bond interactions between daclatasvir and the amino acids of the binding pocket. That causes a structural modification of NS5A, leading to a loss of action and resulting in an inhibition of virion formation. By altering the structure of NS5A, the recruitment of PI4KA and therefore the accumulation of PI4P get disabled. New lipid-drops and membranous components can no longer get recruited by PI4P in the membranous web and the web can no longer maintain. But it is important to mention that daclatasvir does not inhibit PI4KA directly, because it was observed that in cells, which were treated with daclatasvir, PI4P is still present in the plasma membrane and Golgi apparatus. Daclatasvir also does not inhibit the initial PI4KA delocalization induced by NS5A because it was witnessed that daclatasvir had no impact on the function of NS5A within cells expressing only NS5A. It is likely that daclatasvir merely inhibits functions of NS5A associated with other proteins within the HCV replication complex just like the RNA-replicase NS4B. Concluding, daclatasvir presumably only inhibits PI4P hyper-accumulation in the context of full HCV polypeptide expression. This phenomenon is associated with the structure of domain 1 of NS5A. It was observed that domain 1 has two different conformations. Daclatasvir binds to one of these and as a result, locks domain 1 in this conformation. Though, NS5A is still able to bind PI4KA, what can explain the remaining function of NS5A in uninfected cells mentioned before. The second conformation of domain 1, which appears in non-treated cells, is then most likely to be associated with PI4P hyper-accumulation that is necessary for the formation and maintainment of the replication-complex and membranous web. So, PI4KA can still interact with NS5A, but due to the structural blockade,