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Abstract
Virus infections affect plant developmental traits but this aspect of the interaction has not been extensively studied so far. Two strains of Turnip mosaic virus differentially affect Arabidopsis development, especially flower stalk elongation, which allowed phenotypical, cellular, and molecular characterization of the viral determinant, the P3 protein. Transiently expressed wild‐type green fluorescent protein‐tagged P3 proteins of both strains and selected mutants of them revealed important differences in their behaviour as endoplasmic reticulum (ER)‐associated peripheral proteins flowing along the reticulum, forming punctate accumulations. Three‐dimensional (3D) model structures of all expressed P3 proteins were computationally constructed through I‐TASSER protein structure predictions, which were used to compute protein surfaces and map electrostatic potentials to characterize the effect of amino acid changes on features related to protein interactions and to phenotypical and subcellular results. The amino acid at position 279 was the main determinant affecting stalk development. It also determined the speed of ER‐flow of the expressed proteins and their final location. A marked change in the protein surface electrostatic potential correlated with changes in subcellular location. One single amino acid in the P3 viral protein determines all the analysed differential characteristics between strains differentially affecting flower stalk development. A model proposing a role of the protein in the intracellular movement of the viral replication complex, in association with the viral 6K2 protein, is proposed. The type of association between both viral proteins could differ between the strains.
Highlights
Neither P3-green fluorescent protein (GFP) fusion protein co-localized with STtmd-cherry fluorescent protein (ChFP) (PCC: 0.3 for P3[UK1]-GFP; 0.267 for P3[JPN1]-GFP), confirming that transiently expressed Turnip mosaic virus (TuMV) P3-GFPs associate with the endoplasmic reticulum (ER) but are not further exported to the Golgi apparatus (Figure 2)
P3 was identified as the main mediator of flower stalk elongation or arrest in TuMV-infected Arabidopsis plants
Its C-terminal domain contains the determinant of this developmental trait (Sánchez et al, 2015)
Summary
Neither P3-GFP fusion protein co-localized with STtmd-ChFP (PCC: 0.3 for P3[UK1]-GFP; 0.267 for P3[JPN1]-GFP), confirming that transiently expressed TuMV P3-GFPs associate with the ER but are not further exported to the Golgi apparatus (Figure 2). Western blots using an anti-GFP antibody showed that the first treatment (0.1 M Na2CO3) did not affect P3 membrane association, indicating that P3 is not a luminal protein (Figure 3).
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