Bioinformatics Analysis of Mutant Structure and Functional Sites of Foot-and-Mouth Disease virus RNA-dependent RNA polymerase

摘要

Foot-and-mouth disease (FMD) is a kind of highly contagious viral disease caused by the most feared pathogen foot-and-mouth disease virus (FMDV), which belongs to the genus Aphthovirus of picomavirus family and has seven antigenically distinct serotypes The FMDV genome consists of a positive-sense smgle-stranded RNA molecular of approximately 8500 nucleotides. Picomavimses use a protein of 20~24 amino acids, termed VPg, to initiate viral RNA spthesis. During initiation of replication, VPg protein provides the hydroxyl group required by the polymerase to start polynucleotide synthesis. In the process of replication, the first step is the linkage of a nucleotide to the hydroxyl group of an amino acid in the primer protein. This process is catalyzed bythe RNA polymerase which is also responsible for the elongation of the RNA strands. Thus, these polymerases are structurally adapted for using either a protein as a primer. The efficiency of RNA-dependent RNA polymerase (RdRp) m FMDV is critical to thereplication of the viral genomic RNA. Because the mechanism of FMDV RNA replication is identical in vitro and in vivo, it is possible to evaluate the catalytic ability of RdRp using in vitro RNA replication system. The structural and biochemical properties of RdRp in poliovirus of Picomaviridae and hepatitis C virus of Flaviviridae have been studied extensively. Little has been reported on the property of RdRp in FMDV.