Multiple ER‐to‐nucleus stress signaling pathways are activated during
            Plantago asiatica mosaic virus
            and
            Turnip mosaic virus
            infection in
            Arabidopsis thaliana

AbstractThe Arabidopsis thaliana genome encodes several genes that are known or predicted to participate in the formation of stress granules (SG). One family of genes encodes for Ras GTPase-activating protein–binding protein (G3BP)-like proteins. Seven genes were identified, of which one of the members was already shown to interact with plant virus proteins in a previous study. A phylogenetic and tissue-specific expression analysis, including laser-dissected phloem, by qRT-PCRs was performed and the sub-cellular localization of individual AtG3BP::EYFP fluorescent fusion proteins expressed in Nicotiana benthamiana epidermal cells was observed. Individual AtG3BP-protein interactions in planta were studied using the bimolecular fluorescence complementation approach in combination with confocal imaging in living cells. In addition, the early and late induction of G3BP-like expression upon Turnip mosaic virus infection was investigated by RNAseq and qRT-PCR. The results showed a high divergence of transcription frequency in the different plant tissues, promiscuous protein–protein interaction within the G3BP-like gene family, and a general induction by a viral infection with TuMV in A. thaliana. The information gained from these studies leads to a better understanding of stress granules, in particular their molecular mode of action in the plant and their role in plant virus infection.

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Functional Genomic analysis of Turnip mosaic virus infection in Arabidopsis thaliana

10.31274/rtd-180813-16804 ◽

2007 ◽

Author(s):

Chunling Yang

Keyword(s):

Arabidopsis Thaliana ◽

Virus Infection ◽

Mosaic Virus ◽

Genomic Analysis ◽

Turnip Mosaic Virus ◽

Functional Genomic ◽

Functional Genomic Analysis ◽

Mosaic Virus Infection

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Multiple ER-to-nucleus stress signaling pathways become active during Plantago asiatica mosaic virus and Turnip mosaic virus infection in Arabidopsis thaliana

10.1101/786137 ◽

2019 ◽

Cited By ~ 2

Author(s):

Mathieu Gayral ◽

Omar Arias Gaguancela ◽

Evelyn Vasquez ◽

Venura Herath ◽

Mingxiong Pang ◽

...

Keyword(s):

Arabidopsis Thaliana ◽

Protein Folding ◽

Signaling Pathways ◽

Mosaic Virus ◽

Turnip Mosaic Virus ◽

Virus Accumulation ◽

Unfolded Protein ◽

Plantago Asiatica ◽

Protein Response

SummaryEndoplasmic reticulum (ER) stress due to biotic or abiotic stress activates the unfolded protein response (UPR) to restore ER homeostasis. The UPR relies on multiple ER-to-nucleus signaling factors which mainly induce the expression of cytoprotective ER-chaperones. The inositol requiring enzyme (IRE1) along with its splicing target, bZIP60, restrict potyvirus, and potexvirus accumulation. Until now, the involvement of the alternative UPR pathways and the role of UPR to limit virus accumulation have remained elusive. Here, we used the Plantago asiatica mosaic virus (PlAMV) and the Turnip mosaic virus (TuMV) to demonstrate that the potexvirus triple gene block 3 (TGB3) protein and the potyvirus 6K2 protein activate the bZIP17, bZIP28, bZIP60, BAG7, NAC089 and NAC103 signaling in Arabidopsis thaliana. Using the corresponding knock-out mutant lines, we demonstrated that these factors differentially restrict local and systemic virus accumulation. We show that bZIP17, bZIP60, BAG7, and NAC089 are factors in PlAMV infection, whereas bZIP28 and bZIP60 are factors in TuMV infection. TGB3 and 6K2 transient expression in leave reveal that these alternative pathways induce BiPs expression. Finally, using dithiothreitol (DTT) and tauroursodeoxycholic acid (TUDCA) treatment, we demonstrated that the protein folding capacity significantly influences PlAMV accumulation. Together, these results indicate that multiple ER-to-nucleus signaling pathways are activated during virus infection and restrict virus accumulation through increasing protein folding capacity.Significance statementThe IRE1/bZIP60 pathway of unfolded protein response (UPR) is activated by potyviruses and potexviruses, limiting their infection, but the role of alternative UPR pathways is unknown. This study reveals the activation of multiple ER-to-nucleus signaling pathways by the Plantago asiatica mosaic virus and the Turnip mosaic virus. We identify additional signaling pathways serve to restrict virus accumulation through increased protein folding capacity.

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