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

Matthew Bentham1, Kris Holmes, Sophie Forrest

  • 1Institute of Molecular and Cellular Biology, University of Leeds, Leeds, United Kingdom.

Journal of Virology
|December 14, 2011
PubMed

Insights

Foot-and-mouth disease virus (FMDV) RNA polymerase forms unique protein-RNA fibrils essential for replication. These narrower fibrils, dependent on assay components, are inhibited by a specific RNA aptamer.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Viral replication often involves the assembly of specialized structures known as replication factories.
  • Understanding the molecular mechanisms of viral RNA synthesis is crucial for developing antiviral strategies.

Purpose of the Study:

  • To investigate the in vitro self-assembly properties of the foot-and-mouth disease virus (FMDV) RNA-dependent RNA polymerase (RdRp).
  • To characterize the structure and composition of FMDV RdRp higher-order structures and their role in viral replication.

Main Methods:

  • In vitro fibril formation assays using purified FMDV RdRp.
  • Biochemical analysis of fibril composition (protein and RNA).
  • Assessment of fibril formation in the presence and absence of elongation assay components.
  • Inhibition studies using RNA aptamers.

Main Results:

  • FMDV RdRp forms distinct fibrils in vitro.
  • These fibrils are narrower than those of poliovirus polymerase and contain both protein and RNA.
  • Fibril formation is dependent on the presence of all components required for RNA elongation.
  • An inhibitory RNA aptamer effectively prevents fibril formation.

Conclusions:

  • FMDV RdRp self-assembles into functional fibrils crucial for viral RNA replication.
  • The composition and formation conditions of FMDV fibrils offer insights into viral replication factory assembly.
  • Targeting FMDV fibril formation with aptamers presents a potential antiviral therapeutic approach.

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