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Salgueiro, Mariano; Camporeale, Gabriela; Visentin, Araceli; Aran, Martin; Pellizza, Leonardo; Esperante, Sebastián A.; Corbat, Agustín; Grecco, Hernán; Sousa, Belén; Esperón, Ramiro; Borkosky, Silvia S.; de Prat-Gay, Gonzalo
Journal of Molecular Biology/Journal of molecular biology, 2023-Aug-15, Volume: 435, Issue: 16Journal Article
Display omitted •Biophysical principles of RSV virus factory assembly and modulation need to be elucidated.•RSV-P is the scaffold for biomolecular condensation both in vitro and in cells.•RSV-P restores nucleoprotein aggregates into liquid droplets.•RSV-P may act as the “solvent protein” within the viral factories. Viral factories of liquid-like nature serve as sites for transcription and replication in most viruses. The respiratory syncytial virus factories include replication proteins, brought together by the phosphoprotein (P) RNA polymerase cofactor, present across non-segmented negative stranded RNA viruses. Homotypic liquid–liquid phase separation of RSV-P is governed by an α-helical molten globule domain, and strongly self-downmodulated by adjacent sequences. Condensation of P with the nucleoprotein N is stoichiometrically tuned, defining aggregate-droplet and droplet-dissolution boundaries. Time course analysis show small N-P nuclei gradually coalescing into large granules in transfected cells. This behavior is recapitulated in infection, with small puncta evolving to large viral factories, strongly suggesting that P-N nucleation-condensation sequentially drives viral factories. Thus, the tendency of P to undergo phase separation is moderate and latent in the full-length protein but unleashed in the presence of N or when neighboring disordered sequences are deleted. This, together with its capacity to rescue nucleoprotein-RNA aggregates suggests a role as a “solvent-protein”.
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