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Design, synthesis and X-Ray of Foot-and-mouth disease virus (Fluoro)uridylylated peptides linked to the genome (VPgpU and VPgpFU)

AutorCastro, Sonia de ; Ferrer-Orta, Cristina ; Fernández-Cureses, Gloria ; Verdaguer, Núria ; Domingo, Esteban ; Camarasa Rius, María José
Fecha de publicación14-oct-2014
Citación3rd Antiviral Congress (2014)
ResumenFoot-and-mount disease virus (FMDV), belonging to the picornavirus family, is responsible for the highly contagious Foot-and-mounth disease (FMD) of cloven-hoofed bovids. The viral RNA synthesis, is initiated by a viral protein genome-linked (VPg) of 20-24 aminoacids. Unliquely of other picornavirus, FMDV-RNA encodes three distinguishable copies of this protein (VPg1, VPg2, VPg3). Each of them attached to genomic RNA, and therefore believed to be functionally equivalent. During replication initiation, the first step is the binding of a UMP to the hydroxyl group of Tyr3 in the VPg protein. The virally encoded RNA-dependent RNA polymerase (3D) requires the uridylylated VPg form as the primer for both positive- and negative-strand synthesis. 5-Fluorouridine triphosphate (FUTP) is a potent competitive inhibitor of VPg-1 uridylylation. By peptide analysis, a VPg fragment containing FUMP covalently attached to Tyr has been identified. However, the molecular basis of this phenomenon is still unknown. To investigate the role of FUMP, the synthesis and X-ray studies of simplified models of VPg-1 containing U or FU, in peptides of diferent lenghts linked through the hydroxyl group of Tyr3 will be presented. Interestingly, X-ray structure of 3D-pol with a 15-mer peptide FMDV/VPg-FU showed a significant distortion of b9-b11 loop of the polymerase
DescripciónPóster presentado en el 3rd Antiviral Congress, celebrado del 12 al 14 de octubre de 2014 en Amsterdam (Holanda)
URIhttp://hdl.handle.net/10261/129004
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