Brothers in Arms: Structure, Assembly and Function of Arenaviridae Nucleoprotein

Nicolas Papageorgiou1,2, Maria Spiliopoulou3, Thi-Hong Van Nguyen1,2

  • 1Architecture et Fonction des Macromolécules Biologiques, CNRS - UMR 7257, Polytech Case 925, 13009 Marseille, France.

Viruses
|July 26, 2020
PubMed

Insights

Arenaviridae nucleoprotein (NP) is crucial for viral RNA replication and immune evasion. This review highlights NP structure, function, and interactions, identifying it as a key target for antiviral therapies.

Area of Science:

  • Virology
  • Structural Biology
  • Immunology

Background:

  • Arenaviridae are emerging viral pathogens within the Bunyavirales order.
  • Nucleoprotein (NP) is essential for viral RNA genome replication and immune system interference.
  • NP possesses an RNA-binding domain and an exonuclease domain, undergoing conformational changes for RNA encapsidation.

Purpose of the Study:

  • To review recent structural and functional data on Arenaviridae NP.
  • To compare Arenaviridae NP with other Bunyavirales nucleoproteins.
  • To explore structural and functional implications for therapeutic targeting.

Main Methods:

  • Literature review of structural and functional studies.
  • Comparative analysis of Arenaviridae NP and other Bunyavirales nucleoproteins.
  • Evaluation of NP-NP binding modes and NP interactome.

Main Results:

  • Arenaviridae NP has distinct N-terminal RNA-binding and C-terminal exonuclease domains.
  • Conformational changes in NP are vital for RNA encapsidation.
  • NP interactome and exonuclease activity significantly influence viral pathogenesis.

Conclusions:

  • Arenaviridae NP structure and function are critical for viral replication and host interaction.
  • Understanding NP's role in NP-NP binding and its interactome is key.
  • The NP, particularly its exonuclease domain, represents a promising target for novel vaccines and antiviral strategies.

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