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[Structural disorder within the replicative complex of measles virus: functional implications].

J-M Bourhis, Bruno Canard, Sonia Longhi

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Abstract

Measles virus belongs to the Paramyxoviridae family within the Mononegavirales order. Its non segmented, single stranded, negative sense RNA genome is encapsidated by the nucleoprotein (N) to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNApolymerase (L) binds to the nucleocapsid template via its co-factor, the phosphoprotein (P). In this review, we summarize the main experimental data pointing out the abundance of structural disorder within measles virus N and P.We also describe studies indicating that structural disorder is a widespread property in the replicative complex of Paramyxoviridae and, more generally, of Mononegavirales. The functional implications of structural disorder are also discussed. Finally, we propose a model where the flexibility of the disordered N and P domains allows the formation of a tripartite complex (N̊-P-L) during replication, followed by the delivery of N monomers to the nascent genomic RNA chain.

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What this paper is about

Measles virus belongs to the Paramyxoviridae family within the Mononegavirales order. Its non segmented, single stranded, negative sense RNA genome is encapsidated by the nucleoprotein (N) to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNApolymerase (L) binds to the nucleocapsid template via its co-factor, the phosphoprotein (P). In this review, we summarize the main experimental data pointing out the abundance of structural disorder within measles virus N and P.We also describe studies indicating that structural disorder is a widespread property in the replicative complex of Paramyxoviridae and, more generally, of Mononegavirales. The functional implications of structural disorder are also discussed. Finally, we propose a model where the flexibility of the disordered N and P domains allows the formation of a tripartite complex (N̊-P-L) during replication, followed by the delivery of N monomers to the nascent genomic RNA chain.

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Available abstract

Measles virus belongs to the Paramyxoviridae family within the Mononegavirales order. Its non segmented, single stranded, negative sense RNA genome is encapsidated by the nucleoprotein (N) to form a helical nucleocapsid. This ribonucleoproteic complex is the substrate for both transcription and replication. The RNA-dependent RNApolymerase (L) binds to the nucleocapsid template via its co-factor, the phosphoprotein (P). In this review, we summarize the main experimental data pointing out the abundance of structural disorder within measles virus N and P.We also describe studies indicating that structural disorder is a widespread property in the replicative complex of Paramyxoviridae and, more generally, of Mononegavirales. The functional implications of structural disorder are also discussed. Finally, we propose a model where the flexibility of the disordered N and P domains allows the formation of a tripartite complex (N̊-P-L) during replication, followed by the delivery of N monomers to the nascent genomic RNA chain.

Key concepts: Measles virus, Paramyxoviridae, Nucleoprotein, Mononegavirales, Virology, Biology, Morbillivirus, RNA

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