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Updated: Dec 24, 2025

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

Published on: July 27, 2021

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Measles virus nucleo- and phosphoproteins form liquid-like phase-separated compartments that promote nucleocapsid

Serafima Guseva1, Sigrid Milles1, Malene Ringkjøbing Jensen1

  • 1Institut de Biologie Structurale, Université Grenoble Alpes-CEA-CNRS, 71, Avenue des Martyrs, Grenoble, France.

Science Advances
|April 10, 2020
PubMed

Insights

Measles virus proteins form liquid-like compartments in vitro, enhancing RNA encapsidation. This liquid-liquid phase separation is crucial for efficient viral replication and nucleocapsid assembly.

Area of Science:

  • Virology
  • Biochemistry
  • Cell Biology

Background:

  • Viruses form specialized compartments called viral factories for replication.
  • Paramyxoviruses, like measles virus, concentrate genetic and protein material in cellular puncta.

Purpose of the Study:

  • To investigate the in vitro formation of liquid-like organelles by measles virus nucleoproteins (N) and phosphoproteins (P).
  • To elucidate the role of weak interactions and intrinsically disordered domains in phase separation.
  • To understand the impact of liquid-liquid phase separation on RNA encapsidation and viral replication.

Main Methods:

  • In vitro mixing of purified measles virus N and P proteins.
  • Fluorescence microscopy to observe protein dynamics during droplet formation.
  • Nuclear Magnetic Resonance (NMR) spectroscopy to study the thermodynamics of phase separation.
  • RNA co-localization and assembly studies within the formed droplets.

Main Results:

  • Purified N and P proteins of measles virus spontaneously form liquid-like membraneless organelles in vitro.
  • Weak interactions involving intrinsically disordered domains of N and P are critical for phase separation.
  • RNA colocalizes with these droplets and triggers the assembly of nucleocapsid-like particles, enhancing encapsidation rates.
  • Liquid-liquid phase separation accelerates RNA encapsidation compared to dilute conditions.

Conclusions:

  • Measles virus utilizes liquid-liquid phase separation to create functional compartments for efficient replication.
  • The formation of these organelles is driven by weak interactions within intrinsically disordered protein domains.
  • Enhanced RNA encapsidation within these liquid compartments is a key mechanism in the measles virus life cycle.

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