title: Formation of higher-order foot-and-mouth disease virus 3D(pol) complexes is dependent on elongation activity.
abstract: The replication of many viruses involves the formation of higher-order structures or replication "factories." We show that the key replication enzyme of foot-and-mouth disease virus (FMDV), the RNA-dependent RNA polymerase, forms fibrils in vitro. Although there are similarities with previously characterized poliovirus polymerase fibrils, FMDV fibrils are narrower, are composed of both protein and RNA, and, importantly, are seen only when all components of an elongation assay are present. Furthermore, an inhibitory RNA aptamer prevents fibril formation.
authors.affiliation: Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.
authors.forename: Matthew
authors.initials: M
authors.lastname: Bentham
authors.forename: Kris
authors.initials: K
authors.lastname: Holmes
authors.forename: Sophie
authors.initials: S
authors.lastname: Forrest
authors.forename: David J
authors.initials: DJ
authors.lastname: Rowlands
authors.forename: Nicola J
authors.initials: NJ
authors.lastname: Stonehouse
mesh_terms: D002460:Cell Line; D004261:DNA Replication; D029544:Foot-and-Mouth Disease Virus / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D012367:RNA, Viral / Q000235:genetics / Q000378:metabolism; D012324:RNA-Dependent RNA Polymerase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D014764:Viral Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D014779:Virus Replication
chemical_list: D012367:RNA, Viral; D014764:Viral Proteins; D012324:RNA-Dependent RNA Polymerase