Hepatitis C virus NS5A protein function in Progress.docVIP

 PAGE \* MERGEFORMAT 19 Hepatitis C virus NS5A protein function in Progress Author: Zhou dry, Yinfeng Ming Feng Jing-hua [Keywords:] Hepatitis C virus NS5A protein Hepatitis C virus (HCV) can cause hepatitis, cirrhosis and liver cancer and a series of liver disease, and chronic high probability. Currently the world’s still on an upward trend in the number of HCV infections, scientists attach great importance to the study of HCV. HCV has a large open reading frame encoding is about more than 3000 amino acid poly-protein by protease cleavage of more than 10 peptide fragments; amino-terminal for the structural proteins including the core protein, envelope protein E1 and E2, P7 protein; COOH end of the non-structural proteins including NS2, NS3, NS4A, NS4B, NS5A, and NS5B proteins. Based in the NS5A protein in HCV poly-protein precursor of 1973-2419 amino acid region, from 447 amino acids, amino-terminal for the amphiphilic α -helix can be combined with the endoplasmic reticulum. NS5A also contains three similar ProXaaXaaPro motif, these motifs present in many signaling proteins in the formation of extended α -helix, and with the Src homology 3 (SH3) combination of functional areas. According to NS5A phosphorylation of the serine residue in the different levels there are two kinds of mature forms of p56 and p58. A growing number of scientists speculate that NS5A in the HCV proteins may interfere with host cell signaling and immune evasion have a certain role in a number of papers published. In this paper, the role of NS5A protein function and mechanism of research are reviewed. 1 and the relationship between viral replication Lohmann et al [1] the first use of subgenomic replication sub-system study and propose NS5A with RNA replication. Subsequent study further found that the parents membrane NS5A target helix mutation and replication sub-related to split into three helical mutations completely terminate the establishment of G418-resistant replicon clones, me