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Updated: Aug 30, 2026

Generation and Assembly of Virus-Specific Nucleocapsids of the Respiratory Syncytial Virus
Published on: July 27, 2021
Structural disorder and modular organization in Paramyxovirinae N and P
David Karlin1, François Ferron1, Bruno Canard1
1Architecture et Fonction des Macromolécules Biologiques, UMR 6098 CNRS et Université Aix-Marseille I et II, ESIL, Campus de Luminy, 13288 Marseille Cedex 09, France.
Abstract:
The existence and extent of disorder within the replicative complex (N, P and the polymerase, L) of Paramyxovirinae were investigated, drawing on the discovery that the N-terminal moiety of the phosphoprotein (P) and the C-terminal moiety of the nucleoprotein (N) of measles virus are intrinsically unstructured. We show that intrinsic disorder is a widespread property within Paramyxovirinae N and P, using a combination of different computational approaches relying on different physico-chemical concepts. Notably, experimental support that has often gone unnoticed for most of the predictions has been found in the literature. Identification of disordered regions allows the unveiling of a common organization in all Paramyxovirinae P, which are composed of six modules defined on the basis of structure or sequence conservation. The possible functional significance of intrinsic disorder is discussed in the light of experimental data, which show that unstructured regions of P and N are involved in numerous interactions with several protein and protein-RNA partners. This study provides a contribution to the rather poorly investigated field of intrinsically disordered proteins and helps in targeting protein domains for structural studies.
Insights
Paramyxovirinae viruses possess intrinsically disordered proteins crucial for replication. This widespread disorder in nucleoprotein (N) and phosphoprotein (P) underlies their function and interactions.
Area of Science:
- Molecular Biology
- Virology
- Structural Biology
Background:
- The replicative complex of Paramyxovirinae, including nucleoprotein (N), phosphoprotein (P), and polymerase (L), is essential for viral function.
- Previous studies indicated intrinsic disorder in specific domains of measles virus N and P proteins.
Purpose of the Study:
- To investigate the extent and significance of intrinsic disorder within the Paramyxovirinae replicative complex.
- To identify conserved organizational principles and functional roles of disordered regions in N and P proteins.
Main Methods:
- Employed a combination of computational approaches based on diverse physico-chemical principles to predict intrinsic disorder.
- Conducted a thorough literature review to gather experimental evidence supporting computational predictions.
Main Results:
- Intrinsic disorder is a prevalent characteristic of Paramyxovirinae N and P proteins.
- Identified a conserved modular organization in Paramyxovirinae P proteins, comprising six modules based on structural or sequence conservation.
- Unstructured regions of N and P proteins are implicated in multiple interactions with protein and protein-RNA partners.
Conclusions:
- Intrinsic disorder plays a significant role in the function and interactions of the Paramyxovirinae replicative complex.
- This study contributes to understanding intrinsically disordered proteins and aids in identifying target domains for future structural studies.
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