Eukaryotic elongation factor 1A interacts with Turnip mosaic virus RNA-dependent RNA polymerase and VPg-Pro in virus-induced vesicles

Abstract Eukaryotic elongation factor 1-alpha (eEF1A) was identified as an interactor of Turnip mosaic virus (TuMV) RNA-dependent RNA polymerase (RdRp) and VPg-protease (VPg-Pro) using tandem affinity purification and/or in vitro assays. Subcellular fractionation experiments revealed that the level...

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Bibliographic Details
Published in:Virology (New York, N.Y.) N.Y.), 2008-07, Vol.377 (1), p.216-225
Main Authors: Thivierge, Karine, Cotton, Sophie, Dufresne, Philippe J, Mathieu, Isabelle, Beauchemin, Chantal, Ide, Christine, Fortin, Marc G, Laliberté, Jean-François
Format: Article
Language:English
Subjects:
6K-VPg-Pro
Arabidopsis - genetics
Arabidopsis - physiology
Arabidopsis - virology
Arabidopsis Proteins - genetics
Arabidopsis Proteins - physiology
Base Sequence
DNA Primers - genetics
eEF1A
Eukaryotic elongation factor 1 alpha
Host-Pathogen Interactions
Infectious Disease
Nicotiana - genetics
Nicotiana - physiology
Peptide Elongation Factor 1 - genetics
Peptide Elongation Factor 1 - physiology
Peptide Hydrolases - genetics
Peptide Hydrolases - physiology
Plants, Genetically Modified
Potyvirus
Potyvirus - pathogenicity
Potyvirus - physiology
Protein Binding
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
Replication
RNA-dependent RNA polymerase
RNA-Dependent RNA Polymerase - physiology
Translation
Turnip mosaic virus
Virus Replication
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Summary:Abstract Eukaryotic elongation factor 1-alpha (eEF1A) was identified as an interactor of Turnip mosaic virus (TuMV) RNA-dependent RNA polymerase (RdRp) and VPg-protease (VPg-Pro) using tandem affinity purification and/or in vitro assays. Subcellular fractionation experiments revealed that the level of eEF1A substantially increased in membrane fractions upon TuMV infection. Replication of TuMV occurs in cytoplasmic membrane vesicles, which are induced by 6K-VPg-Pro. Confocal microscopy indicated that eEF1A was included in these vesicles. To confirm that eEF1A was found in replication vesicles, we constructed an infectious recombinant TuMV that contains an additional copy of the 6K protein fused to the green fluorescent protein (GFP). In cells infected with this recombinant TuMV, fluorescence emitted by 6KGFP was associated with cytoplasmic membrane vesicles that contained VPg-Pro, the eukaryotic initiation factor (iso) 4E, the poly(A)-binding protein, the heat shock cognate 70-3 protein, and eEF1A. These results suggest that TuMV-induced membrane vesicles host at least three plant translation factors in addition to the viral replication proteins.
ISSN:0042-6822
1096-0341
DOI:10.1016/j.virol.2008.04.015