Enrichment of Phosphatidylethanolamine in Viral Replication Compartments via Co-opting the Endosomal Rab5 Small GTPase by a Positive-Strand RNA Virus

Positive-strand RNA viruses build extensive membranous replication compartments to support replication and protect the virus from antiviral responses by the host. These viruses require host factors and various lipids to form viral replication complexes (VRCs). The VRCs built by Tomato bushy stunt vi...

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Bibliographic Details
Published in:PLoS biology 2016-10, Vol.14 (10), p.e2000128-e2000128
Main Authors: Xu, Kai, Nagy, Peter D
Format: Article
Language:English
Subjects:
Biology and Life Sciences
Cell Compartmentation
Colleges & universities
Endosomes - enzymology
Funding
Guanosine triphosphatase
Health aspects
Lasers
Lipids
Localization
Membranes
Microscopy
Phosphatidylethanolamines - metabolism
Plant pathology
Proteins
rab5 GTP-Binding Proteins - metabolism
Recruitment
Research and Analysis Methods
RNA viruses
Software
Tombusviridae
Tombusvirus - physiology
Virus Replication
Viruses
Yeast
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Description
Summary:Positive-strand RNA viruses build extensive membranous replication compartments to support replication and protect the virus from antiviral responses by the host. These viruses require host factors and various lipids to form viral replication complexes (VRCs). The VRCs built by Tomato bushy stunt virus (TBSV) are enriched with phosphatidylethanolamine (PE) through a previously unknown pathway. To unravel the mechanism of PE enrichment within the TBSV replication compartment, in this paper, the authors demonstrate that TBSV co-opts the guanosine triphosphate (GTP)-bound active form of the endosomal Rab5 small GTPase via direct interaction with the viral replication protein. Deletion of Rab5 orthologs in a yeast model host or expression of dominant negative mutants of plant Rab5 greatly decreases TBSV replication and prevents the redistribution of PE to the sites of viral replication. We also show that enrichment of PE in the viral replication compartment is assisted by actin filaments. Interestingly, the closely related Carnation Italian ringspot virus, which replicates on the boundary membrane of mitochondria, uses a similar strategy to the peroxisomal TBSV to hijack the Rab5-positive endosomes into the viral replication compartments. Altogether, usurping the GTP-Rab5-positive endosomes allows TBSV to build a PE-enriched viral replication compartment, which is needed to support peak-level replication. Thus, the Rab family of small GTPases includes critical host factors assisting VRC assembly and genesis of the viral replication compartment.
ISSN:1545-7885
1544-9173
1545-7885
DOI:10.1371/journal.pbio.2000128