RNA transport during TMV cell-to-cell movement

Peña, Eduardo José; Heinlein, Manfred

doi:10.3389/fpls.2012.00193

Cited by 45 publications

(43 citation statements)

References 99 publications

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“…What is not understood is how the virions move from the site of synthesis, the P6 IBs, to the plasmodesmata. For many viruses, models for intracellular movement of the virus have involved the viral MP (Epel, 2009;Harries et al, 2010;Schoelz et al, 2011;Patarroyo et al, 2012;Peña and Heinlein, 2012;Tilsner and Oparka, 2012;Liu and Nelson, 2013). However, in the case of CaMV, Stavolone et al (2005) emphasize that the CaMV MP and virion/VAP complex may travel independently to the plasmodesmata and may first encounter each other at the entrance to the plasmodesmata.…”

Section: Discussionmentioning

confidence: 99%

“…However, even with the latter model, there is ample evidence that the viral proteins necessary for replication or cell-to-cell movement utilize intracellular trafficking pathways within the cell to become positioned at the plasmodesma. These pathways may involve microfilaments, microtubules, or specific endomembranes that participate in macromolecular transport pathways, or combinations of these elements (Harries et al, 2010;Schoelz et al, 2011;Patarroyo et al, 2012;Peña and Heinlein, 2012;Tilsner and Oparka 2012;Liu and Nelson, 2013).…”

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confidence: 99%

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Association of the P6 Protein of Cauliflower mosaic virus with Plasmodesmata and Plasmodesmal Proteins

et al. 2014

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The P6 protein of Cauliflower mosaic virus (CaMV) is responsible for the formation of inclusion bodies (IBs), which are the sites for viral gene expression, replication, and virion assembly. Moreover, recent evidence indicates that ectopically expressed P6 inclusion-like bodies (I-LBs) move in association with actin microfilaments. Because CaMV virions accumulate preferentially in P6 IBs, we hypothesized that P6 IBs have a role in delivering CaMV virions to the plasmodesmata. We have determined that the P6 protein interacts with a C2 calcium-dependent membrane-targeting protein (designated Arabidopsis [Arabidopsis thaliana] Soybean Response to Cold [AtSRC2.2]) in a yeast (Saccharomyces cerevisiae) two-hybrid screen and have confirmed this interaction through coimmunoprecipitation and colocalization assays in the CaMV host Nicotiana benthamiana. An AtSRC2.2 protein fused to red fluorescent protein (RFP) was localized to the plasma membrane and specifically associated with plasmodesmata. The AtSRC2.2-RFP fusion also colocalized with two proteins previously shown to associate with plasmodesmata: the host protein Plasmodesmata-Localized Protein1 (PDLP1) and the CaMV movement protein (MP). Because P6 I-LBs colocalized with AtSRC2.2 and the P6 protein had previously been shown to interact with CaMV MP, we investigated whether P6 I-LBs might also be associated with plasmodesmata. We examined the colocalization of P6-RFP I-LBs with PDLP1-green fluorescent protein (GFP) and aniline blue (a stain for callose normally observed at plasmodesmata) and found that P6-RFP I-LBs were associated with each of these markers. Furthermore, P6-RFP coimmunoprecipitated with PDLP1-GFP. Our evidence that a portion of P6-GFP I-LBs associate with AtSRC2.2 and PDLP1 at plasmodesmata supports a model in which P6 IBs function to transfer CaMV virions directly to MP at the plasmodesmata.Through the years, numerous studies have focused on the characterization of viral replication sites within the cell, as well as how plant virus movement proteins (MPs) modify the plasmodesmata to facilitate cell-tocell movement (for review, see Benitez-Alfonso et al.,

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Association of the P6 Protein of Cauliflower mosaic virus with Plasmodesmata and Plasmodesmal Proteins

et al. 2014

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“…Viral replication takes place in the proximity of the endoplasmic reticulum (ER) membranes, into the so-called 'viral replication factories' of which the MP is a pivotal component (Beachy and Heinlein, 2000;Asurmendi et al, 2004). The MP directs the vRNA for its passage through the plasmodesmata (Peña and Heinlein, 2012), becoming the next viral component required to initiate the intermediate stage of the dynamic viral replication. This protein is located predominantly at the leading front of infection, controlling plasmodesmata gating in a temporal manner (Oparka et al, 1997).…”

Section: Tmv Structure and Dynamic Overview Of Viral Replication Processmentioning

confidence: 99%

Modulation of host plant immunity by Tobamovirus proteins

Conti

Rodríguez

Venturuzzi

et al. 2016

Ann Bot

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Background To establish successful infection, plant viruses produce profound alterations of host physiology, disturbing unrelated endogenous processes and contributing to the development of disease. In tobamoviruses, emerging evidence suggests that viral-encoded proteins display a great variety of functions beyond the canonical roles required for virus structure and replication. Among these, their modulation of host immunity appears to be relevant in infection progression.Scope In this review, some recently described effects on host plant physiology of Tobacco mosaic virus (TMV)-encoded proteins, namely replicase, movement protein (MP) and coat protein (CP), are summarized. The discussion is focused on the effects of each viral component on the modulation of host defense responses, through mechanisms involving hormonal imbalance, innate immunity modulation and antiviral RNA silencing. These effects are described taking into consideration the differential spatial distribution and temporality of viral proteins during the dynamic process of replication and spread of the virus.Conclusion In discussion of these mechanisms, it is shown that both individual and combined effects of viralencoded proteins contribute to the development of the pathogenesis process, with the host plant's ability to control infection to some extent potentially advantageous to the invading virus.

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“…According to the current model, TMV movement occurs in form of MP TMV -containing viral ribonucleoprotein/replication complexes that are transported in association with the ER to the PD for intercellular spread (Niehl and Heinlein, 2011;Peña and Heinlein, 2012). Since MP is essential for this process, we expected that TMV movement should be inhibited if CDC48 activity removes MP from the ER upon introduction into cells at the leading front of infection.…”

Section: Expression Of Cdc48b Ahead Of Infection Reduces the Size Of mentioning

confidence: 99%

“…During the course of infection, as well as when ectopically expressed, the MP associates with PD, the ER/actin network, and microtubules (Heinlein et al, 1995Reichel and Beachy, 1998;Wright et al, 2007;Sambade et al, 2008;Hofmann et al, 2009;Boutant et al, 2010;Peña and Heinlein, 2012;Supplemental Fig. S1).…”

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Control of Tobacco mosaic virus Movement Protein Fate by CELL-DIVISION-CYCLE Protein48

et al. 2012

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Like many other viruses, Tobacco mosaic virus replicates in association with the endoplasmic reticulum (ER) and exploits this membrane network for intercellular spread through plasmodesmata (PD), a process depending on virus-encoded movement protein (MP). The movement process involves interactions of MP with the ER and the cytoskeleton as well as its targeting to PD. Later in the infection cycle, the MP further accumulates and localizes to ER-associated inclusions, the viral factories, and along microtubules before it is finally degraded. Although these patterns of MP accumulation have been described in great detail, the underlying mechanisms that control MP fate and function during infection are not known. Here, we identify CELL-DIVISION-CYCLE protein48 (CDC48), a conserved chaperone controlling protein fate in yeast (Saccharomyces cerevisiae) and animal cells by extracting protein substrates from membranes or complexes, as a cellular factor regulating MP accumulation patterns in plant cells. We demonstrate that Arabidopsis (Arabidopsis thaliana) CDC48 is induced upon infection, interacts with MP in ER inclusions dependent on the MP N terminus, and promotes degradation of the protein. We further provide evidence that CDC48 extracts MP from ER inclusions to the cytosol, where it subsequently accumulates on and stabilizes microtubules. We show that virus movement is impaired upon overexpression of CDC48, suggesting that CDC48 further functions in controlling virus movement by removal of MP from the ER transport pathway and by promoting interference of MP with microtubule dynamics. CDC48 acts also in response to other proteins expressed in the ER, thus suggesting a general role of CDC48 in ER membrane maintenance upon ER stress.

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RNA transport during TMV cell-to-cell movement

Cited by 45 publications

References 99 publications

Association of the P6 Protein of Cauliflower mosaic virus with Plasmodesmata and Plasmodesmal Proteins

Association of the P6 Protein of Cauliflower mosaic virus with Plasmodesmata and Plasmodesmal Proteins

Modulation of host plant immunity by Tobamovirus proteins

Control of Tobacco mosaic virus Movement Protein Fate by CELL-DIVISION-CYCLE Protein48

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