Formation of higher-order foot-and-mouth disease virus 3D(pol) complexes is dependent on elongation activity

J Virol. 2012 Feb;86(4):2371-4. doi: 10.1128/JVI.05696-11. Epub 2011 Dec 7.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Cell Line
  • DNA Replication*
  • Foot-and-Mouth Disease Virus / chemistry
  • Foot-and-Mouth Disease Virus / enzymology*
  • Foot-and-Mouth Disease Virus / genetics
  • Foot-and-Mouth Disease Virus / physiology
  • RNA, Viral / genetics
  • RNA, Viral / metabolism
  • RNA-Dependent RNA Polymerase / chemistry*
  • RNA-Dependent RNA Polymerase / genetics
  • RNA-Dependent RNA Polymerase / metabolism*
  • Viral Proteins / chemistry*
  • Viral Proteins / genetics
  • Viral Proteins / metabolism
  • Virus Replication

Substances

  • RNA, Viral
  • Viral Proteins
  • RNA-Dependent RNA Polymerase