Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.

Both cellular and viral proteins can undergo phase separation and form membraneless compartments that concentrate biomolecules. The p26 movement protein from single-stranded, positive-sense Pea enation mosaic virus 2 (PEMV2) separates into a dense phase in nucleoli where p26 and related orthologues...

Descripción completa

Guardado en:

Detalles Bibliográficos
Autores principales:	Shelby L Brown, Dana J Garrison, Jared P May
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2021
Materias:	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
Acceso en línea:	https://doaj.org/article/1fa160cbc5d04bc9bf2afa384d3cf5b5
Etiquetas:	Agregar Etiqueta Sin Etiquetas, Sea el primero en etiquetar este registro!

id	oai:doaj.org-article:1fa160cbc5d04bc9bf2afa384d3cf5b5
record_format	dspace
spelling	oai:doaj.org-article:1fa160cbc5d04bc9bf2afa384d3cf5b52021-12-02T20:00:08ZPhase separation of a plant virus movement protein and cellular factors support virus-host interactions.1553-73661553-737410.1371/journal.ppat.1009622https://doaj.org/article/1fa160cbc5d04bc9bf2afa384d3cf5b52021-09-01T00:00:00Zhttps://doi.org/10.1371/journal.ppat.1009622https://doaj.org/toc/1553-7366https://doaj.org/toc/1553-7374Both cellular and viral proteins can undergo phase separation and form membraneless compartments that concentrate biomolecules. The p26 movement protein from single-stranded, positive-sense Pea enation mosaic virus 2 (PEMV2) separates into a dense phase in nucleoli where p26 and related orthologues must interact with fibrillarin (Fib2) as a pre-requisite for systemic virus movement. Using in vitro assays, viral ribonucleoprotein complexes containing p26, Fib2, and PEMV2 genomic RNAs formed droplets that may provide the basis for self-assembly in planta. Mutating basic p26 residues (R/K-G) blocked droplet formation and partitioning into Fib2 droplets or the nucleolus and prevented systemic movement of a Tobacco mosaic virus (TMV) vector in Nicotiana benthamiana. Mutating acidic residues (D/E-G) reduced droplet formation in vitro, increased nucleolar retention 6.5-fold, and prevented systemic movement of TMV, thus demonstrating that p26 requires electrostatic interactions for droplet formation and charged residues are critical for nucleolar trafficking and virus movement. p26 readily partitioned into stress granules (SGs), which are membraneless compartments that assemble by clustering of the RNA binding protein G3BP following stress. G3BP is upregulated during PEMV2 infection and over-expression of G3BP restricted PEMV2 RNA accumulation >20-fold. Deletion of the NTF2 domain that is required for G3BP condensation restored PEMV2 RNA accumulation >4-fold, demonstrating that phase separation enhances G3BP antiviral activity. These results indicate that p26 partitions into membraneless compartments with either proviral (Fib2) or antiviral (G3BP) factors.Shelby L BrownDana J GarrisonJared P MayPublic Library of Science (PLoS)articleImmunologic diseases. AllergyRC581-607Biology (General)QH301-705.5ENPLoS Pathogens, Vol 17, Iss 9, p e1009622 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5
spellingShingle	Immunologic diseases. Allergy RC581-607 Biology (General) QH301-705.5 Shelby L Brown Dana J Garrison Jared P May Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
description	Both cellular and viral proteins can undergo phase separation and form membraneless compartments that concentrate biomolecules. The p26 movement protein from single-stranded, positive-sense Pea enation mosaic virus 2 (PEMV2) separates into a dense phase in nucleoli where p26 and related orthologues must interact with fibrillarin (Fib2) as a pre-requisite for systemic virus movement. Using in vitro assays, viral ribonucleoprotein complexes containing p26, Fib2, and PEMV2 genomic RNAs formed droplets that may provide the basis for self-assembly in planta. Mutating basic p26 residues (R/K-G) blocked droplet formation and partitioning into Fib2 droplets or the nucleolus and prevented systemic movement of a Tobacco mosaic virus (TMV) vector in Nicotiana benthamiana. Mutating acidic residues (D/E-G) reduced droplet formation in vitro, increased nucleolar retention 6.5-fold, and prevented systemic movement of TMV, thus demonstrating that p26 requires electrostatic interactions for droplet formation and charged residues are critical for nucleolar trafficking and virus movement. p26 readily partitioned into stress granules (SGs), which are membraneless compartments that assemble by clustering of the RNA binding protein G3BP following stress. G3BP is upregulated during PEMV2 infection and over-expression of G3BP restricted PEMV2 RNA accumulation >20-fold. Deletion of the NTF2 domain that is required for G3BP condensation restored PEMV2 RNA accumulation >4-fold, demonstrating that phase separation enhances G3BP antiviral activity. These results indicate that p26 partitions into membraneless compartments with either proviral (Fib2) or antiviral (G3BP) factors.
format	article
author	Shelby L Brown Dana J Garrison Jared P May
author_facet	Shelby L Brown Dana J Garrison Jared P May
author_sort	Shelby L Brown
title	Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
title_short	Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
title_full	Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
title_fullStr	Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
title_full_unstemmed	Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
title_sort	phase separation of a plant virus movement protein and cellular factors support virus-host interactions.
publisher	Public Library of Science (PLoS)
publishDate	2021
url	https://doaj.org/article/1fa160cbc5d04bc9bf2afa384d3cf5b5
work_keys_str_mv	AT shelbylbrown phaseseparationofaplantvirusmovementproteinandcellularfactorssupportvirushostinteractions AT danajgarrison phaseseparationofaplantvirusmovementproteinandcellularfactorssupportvirushostinteractions AT jaredpmay phaseseparationofaplantvirusmovementproteinandcellularfactorssupportvirushostinteractions
_version_	1718375708538961920

Phase separation of a plant virus movement protein and cellular factors support virus-host interactions.

Ejemplares similares