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Processing and assembly of foot-and-mouth disease virus proteins using subgenomic RNA

B E Clarke1, D V Sangar

  • 1Department of Virology, Wellcome Biotechnology Limited, Beckenham, U.K.

The Journal of General Virology
|September 1, 1988
PubMed

Insights

Researchers studied foot-and-mouth disease virus (FMDV) processing using recombinant DNA. They found structural proteins assemble into empty particles, with 3C protease playing a key role, but not mediating the primary P1-P2 cleavage.

Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Foot-and-mouth disease virus (FMDV) is a significant pathogen.
  • Understanding viral protein processing and assembly is crucial for FMDV control.
  • Recombinant DNA technology offers tools to study viral mechanisms.

Purpose of the Study:

  • To investigate the mechanisms of proteolytic processing and assembly in FMDV.
  • To elucidate the role of specific viral proteases in these processes.
  • To characterize the requirements for FMDV structural protein processing and particle formation.

Main Methods:

  • Construction of recombinant DNA clones for FMDV.
  • Synthesis of RNA transcripts using SP6 polymerase.
  • In vitro translation of RNA transcripts in rabbit reticulocyte lysates.
  • Analysis of proteolytic processing and assembly of viral proteins.

Main Results:

  • Efficient translation of FMDV RNA occurred without 5' untranslated sequences.
  • FMDV structural proteins were processed in the presence of functional 3C protease, which acted in trans.
  • 3C protease specificity extended beyond Glu-Gly bonds.
  • Processed structural proteins assembled into subviral structures resembling empty particles.
  • The primary P1-P2 cleavage was not mediated by 3C or L protease.
  • Evidence suggested a rapid 2A-2B cleavage, followed by 3C-mediated P1/2A junction cleavage.

Conclusions:

  • FMDV structural protein processing and assembly can be studied using recombinant DNA and in vitro translation systems.
  • 3C protease is essential for processing FMDV structural proteins and facilitates assembly into empty particles.
  • The primary cleavage site (P1-P2) is processed through a mechanism distinct from 3C or L protease activity, involving sequential cleavages.

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