Turnip Mosaic Virus Components Are Released into the Extracellular Space by Vesicles in Infected Leaves

Movahed, Nooshin; Cabanillas, Daniel Garcia; Wan, Juan; Vali, Hojatollah; Laliberté, Jean‐François; Zheng, Huanquan

doi:10.1104/pp.19.00381

Cited by 85 publications

(86 citation statements)

References 72 publications

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“…MVBs, next to cytoplasmic proteins also carry small RNAs and serve as another alternative route for secretion of LPs [24]. The amount of EVs was enhanced after infection with powdery mildew fungus in barley [25], Pseudomonas syringae in Arabidopsis plants [26,27], Botrytis cinerea in Arabidopsis cells or Turnip mosaic virus infection of tobacco leaves [28]. Recently, Rutter and Innes (2017) examined the proteome of EVs from Arabidopsis, indicating the presence of many stress responsive proteins, including lectins, characteristic for biotic and abiotic stresses [27].…”

Section: Introductionmentioning

confidence: 99%

The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion

Dubiel

Coninck

Osterne

et al. 2020

IJMS

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Stress granules are cytoplasmic compartments, which serve as mRNA storage units during stress, therefore regulating translation. The Arabidopsis thaliana lectin ArathEULS3 has been widely described as a stress inducible gene. This study aimed to examine in detail the localization of ArathEULS3 lectin in normal and stressed cells. Colocalization experiments revealed that the nucleo-cytoplasmic lectin ArathEULS3 relocates to stress granules after stress. The ArathEULS3 sequence encodes a protein with a EUL lectin domain and an N-terminal domain with unknown structure and function. Bioinformatics analyses showed that the N-terminal domain sequence contains intrinsically disordered regions and likely does not exhibit a stable protein fold. Plasmolysis experiments indicated that ArathEULS3 also localizes to the apoplast, suggesting that this protein might follow an unconventional route for secretion. As part of our efforts we also investigated the interactome of ArathEULS3 and identified several putative interaction partners important for the protein translation process.

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Section: Introductionmentioning

confidence: 99%

The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion

Dubiel

Coninck

Osterne

et al. 2020

IJMS

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“…2), P3C (13), or PIPO (20) are also defective in the intercellular movement of potyviruses, it is possible that anchoring the replicative 6K2 vesicles or aggregates to the PD-located CI inclusions via the sequential interactions between CI, P3N-PIPO, 6K2, and P3 is a critical step in cell-to-cell movement. 6K2 vesicles can move between cells and enter into the extracellular space by exocytosis (46,47). It will be interesting to investigate the role of these multipartite interactions among 6K2, P3, P3N-PIPO, and CI in this process.…”

Section: Discussionmentioning

confidence: 99%

P3N-PIPO Interacts with P3 via the Shared N-Terminal Domain To Recruit Viral Replication Vesicles for Cell-to-Cell Movement

Chai

Liu

et al. 2020

J Virol

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P3N-PIPO, the only dedicated movement protein (MP) of potyviruses, directs cylindrical inclusion (CI) protein from the cytoplasm to the plasmodesma (PD), where CI forms conical structures for intercellular movement. To better understand potyviral cell-to-cell movement, we further characterized P3N-PIPO using Turnip mosaic virus (TuMV) as a model virus. We found that P3N-PIPO interacts with P3 via the shared P3N domain and that TuMV mutants lacking the P3N domain of either P3N-PIPO or P3 are defective in cell-to-cell movement. Moreover, we found that the PIPO domain of P3N-PIPO is sufficient to direct CI to the PD, whereas the P3N domain is necessary for localization of P3N-PIPO to 6K2-labeled vesicles or aggregates. Finally, we discovered that the interaction between P3 and P3N-PIPO is essential for the recruitment of CI to cytoplasmic 6K2-containing structures and the association of 6K2-containing structures with PD-located CI inclusions. These data suggest that both P3N and PIPO domains are indispensable for potyviral cell-to-cell movement and that the 6K2 vesicles in proximity to PDs resulting from multipartite interactions among 6K2, P3, P3N-PIPO, and CI may also play an essential role in this process. IMPORTANCE Potyviruses include numerous economically important viruses that represent approximately 30% of known plant viruses. However, there is still limited information about the mechanism of potyviral cell-to-cell movement. Here, we show that P3N-PIPO interacts with and recruits CI to the PD via the PIPO domain and interacts with P3 via the shared P3N domain. We further report that the interaction of P3N-PIPO and P3 is associated with 6K2 vesicles and brings the 6K2 vesicles into proximity with PD-located CI structures. These results support the notion that the replication and cell-to-cell movement of potyviruses are processes coupled by anchoring viral replication complexes at the entrance of PDs, which greatly increase our knowledge of the intercellular movement of potyviruses.

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“…In plants, EVs are known to contain antimicrobial compounds and defense-related proteins, and participate in localized immune responses to invading fungal and bacterial pathogens (Rutter and Innes, 2018). In this study (Movahed et al, 2019), the proteome of infected N. benthamiana and Arabidopsis EVs was investigated using improved EV isolation methods (Rutter and Innes, 2017). Among those host proteins found exclusively in EVs of infected plants, several were identified that are known to be involved in TuMV replication, as well as enzymes involved in lipid and secondary metabolism biosynthesis pathways.…”

Section: Viruses On the Move In The Extracellular Spacementioning

confidence: 99%

“…A, apoplast; Chl, chloroplast; CI, cylindrical inclusion body; CV, cluster of vesicles; CW, cell wall; P, plasmodesmata; PM, plasma membrane. Images adapted from figures 1, 3, and 4 inMovahed et al (2019).…”

mentioning

confidence: 99%

Viruses on the Move in the Extracellular Space

Richardson

2019

Plant Physiol.

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Turnip Mosaic Virus Components Are Released into the Extracellular Space by Vesicles in Infected Leaves

Cited by 85 publications

References 72 publications

The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion

The ArathEULS3 Lectin Ends up in Stress Granules and Can Follow an Unconventional Route for Secretion

P3N-PIPO Interacts with P3 via the Shared N-Terminal Domain To Recruit Viral Replication Vesicles for Cell-to-Cell Movement

Viruses on the Move in the Extracellular Space

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