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Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
09:08

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus

Published on: July 27, 2021

Direct interaction between two viral proteins, the nonstructural protein 2C and the capsid protein VP3, is required

Ying Liu1, Chunling Wang, Steffen Mueller

  • 1Department of Molecular Genetics and Microbiology, School of Medicine, Stony Brook University, Stony Brook, New York, United States of America.

Plos Pathogens
|September 25, 2010
PubMed

Insights

Viral morphogenesis specificity is driven by protein interactions, not RNA signals. Poliovirus (PV) non-structural protein 2C(ATPase) directly binds capsid protein VP3, ensuring correct viral particle assembly.

Area of Science:

  • Virology
  • Molecular Biology
  • Structural Biology

Background:

  • The precise mechanism governing the morphogenesis of plus-stranded RNA viruses, specifically enteroviruses like poliovirus (PV), remains elusive despite extensive research.
  • Previous attempts to pinpoint an RNA encapsidation signal have been unsuccessful, leaving the specificity of viral particle formation unexplained.

Purpose of the Study:

  • To elucidate the mechanism of poliovirus (PV) encapsidation specificity.
  • To investigate the role of protein-protein interactions in viral morphogenesis, particularly the involvement of non-structural protein 2C(ATPase).

Main Methods:

  • Construction and analysis of a novel reporter virus system using chimeric viruses between PV and C-cluster coxsackie viruses (C-CAVs).
  • Genetic manipulation involving single and double mutations in capsid protein VP3 and 2C(ATPase).
  • Biochemical assays to confirm direct protein-protein interactions.

Main Results:

  • A chimera of C-cluster coxsackie virus 20 (C-CAV20) and PV non-structural proteins showed blocked encapsidation, despite successful genome replication.
  • Encapsidation was rescued by mutations in either C-CAV20's VP3 or PV's 2C(ATPase), with dual mutations restoring wild-type kinetics.
  • Biochemical evidence confirmed direct interaction between 2C(ATPase) and VP3 from both PV and C-CAV20.
  • Chimeras between different C-CAVs were blocked unless capsid and 2C(ATPase) originated from the same virus, highlighting specificity.

Conclusions:

  • Viral morphogenesis specificity is mediated by direct protein-protein interactions, specifically between 2C(ATPase) and capsid proteins like VP3, rather than RNA signals.
  • This interaction mechanism ensures that newly synthesized viral genomes are efficiently packaged at the replication site.

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