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Chimeric picornavirus polyproteins demonstrate a common 3C proteinase substrate specificity.

P G Dewalt1, M A Lawson, R J Colonno

  • 1Department of Microbiology and Molecular Genetics, College of Medicine, University of California, Irvine 92717.

Journal of Virology
|August 1, 1989
PubMed
Summary

Heterologous 3C proteinases from other picornaviruses can process poliovirus nonstructural proteins. However, they cannot process poliovirus capsid precursors, suggesting common conformational determinants for viral protein processing.

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Area of Science:

  • Virology
  • Molecular Biology
  • Biochemistry

Background:

  • Picornaviruses, including poliovirus, human rhinovirus 14, and coxsackievirus B3, rely on specific proteinases for viral replication.
  • The 3C proteinase is crucial for cleaving viral polyproteins into functional units.
  • Understanding the substrate specificity of viral proteinases is key to deciphering viral replication mechanisms.

Purpose of the Study:

  • To investigate the cross-species proteolytic processing capabilities of 3C proteinases from human rhinovirus 14 and coxsackievirus B3 on poliovirus precursors.
  • To determine if heterologous 3C proteinases can functionally substitute for poliovirus 3C proteinase in processing specific viral proteins.

Main Methods:

  • Construction of chimeric picornavirus cDNA genomes by substituting the poliovirus 3C coding region with alleles from human rhinovirus 14 or coxsackievirus B3.

Related Experiment Videos

  • In vitro translation and proteolytic processing assays using polypeptides encoded by the chimeric genomes.
  • Analysis of the substrate specificity of heterologous 3C proteinases on poliovirus-specific polypeptide precursors.

    • Main Results:

    • Heterologous 3C proteinases from human rhinovirus 14 and coxsackievirus B3 successfully processed poliovirus P2 region nonstructural proteins.
    • These heterologous 3C proteinases were unable to recognize and cleave poliovirus-specific processing sites within the viral capsid precursor.
    • The P2 region cleavage sites showed limited amino acid conservation, suggesting conformational determinants are critical for 3C-mediated processing.

    Conclusions:

    • The 3C proteinases exhibit distinct substrate specificities, with functional substitution observed for nonstructural protein processing but not capsid protein processing.
    • Common conformational determinants, rather than strict amino acid sequence conservation, are likely essential for 3C proteinase recognition of cleavage sites.
    • These findings provide insights into the molecular mechanisms governing picornavirus polyprotein processing and viral evolution.