Movement of Viruses to and Through Plasmodesmata

Nelson, Richard S.

doi:10.1002/9780470988572.ch9

Cited by 10 publications

(10 citation statements)

References 111 publications

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“…Recent information supports the involvement of the endomembrane system in virus intracellular and intercellular movement (for review, see Beachy, 1998, 2000;Morozov and Solovyev, 2003;Nelson, 2005;Verchot-Lubicz, 2005 Article, publication date, and citation information can be found at www.plantphysiol.org/cgi…”

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confidence: 97%

“…These invaginations, or spherules, are centers for virus replication and contain the BMV 2a protein and viral RNA (Schwartz et al, 2004). It was suggested that the BMV-induced spherules resemble budding retrovirus cores and that these membrane invaginations containing VRCs have a place in virus evolution (Schwartz et al, 2002(Schwartz et al, , 2004.Recent information supports the involvement of the endomembrane system in virus intracellular and intercellular movement (for review, see Beachy, 1998, 2000;Morozov and Solovyev, 2003;Nelson, 2005;Verchot-Lubicz, 2005 Article, publication date, and citation information can be found at www.plantphysiol.org/cgi …”

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confidence: 99%

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The Potato Virus X TGBp2 Movement Protein Associates with Endoplasmic Reticulum-Derived Vesicles during Virus Infection

et al. 2005

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The green fluorescent protein (GFP) gene was fused to the potato virus X (PVX) TGBp2 gene, inserted into either the PVX infectious clone or pRTL2 plasmids, and used to study protein subcellular targeting. In protoplasts and plants inoculated with PVX-GFP:TGBp2 or transfected with pRTL2-GFP:TGBp2, fluorescence was mainly in vesicles and the endoplasmic reticulum (ER). During late stages of virus infection, fluorescence became increasingly cytosolic and nuclear. Protoplasts transfected with PVX-GFP:TGBp2 or pRTL2-GFP:TGBp2 were treated with cycloheximide and the decline of GFP fluorescence was greater in virus-infected protoplasts than in pRTL2-GFP:TGBp2-transfected protoplasts. Thus, protein instability is enhanced in virusinfected protoplasts, which may account for the cytosolic and nuclear fluorescence during late stages of infection. Immunogold labeling and electron microscopy were used to further characterize the GFP:TGBp2-induced vesicles. Label was associated with the ER and vesicles, but not the Golgi apparatus. The TGBp2-induced vesicles appeared to be ER derived. For comparison, plasmids expressing GFP fused to TGBp3 were transfected to protoplasts, bombarded to tobacco leaves, and studied in transgenic leaves. The GFP:TGBp3 proteins were associated mainly with the ER and did not cause obvious changes in the endomembrane architecture, suggesting that the vesicles reported in GFP:TGBp2 studies were induced by the PVX TGBp2 protein. In double-labeling studies using confocal microscopy, fluorescence was associated with actin filaments, but not with Golgi vesicles. We propose a model in which reorganization of the ER and increased protein degradation is linked to plasmodesmata gating.Plant viruses use the cellular endomembrane system to support virus replication (Schaad et al., 1997;Reichel and Beachy, 1998;Carette et al., 2002aCarette et al., , 2002bSchwartz et al., 2002). Among positive-strand RNA viruses, the viral replicase is typically anchored to membranes associated with the endoplasmic reticulum (ER), the endocytic pathway, or cellular organelles (Rubino and Russo, 1998;Mas and Beachy, 1999;Rubino et al., 2001;Schwartz et al., 2002Schwartz et al., , 2004. Many viral replicationassociated proteins cause reorganization of cellular membranes with the purpose of creating centers that protect the viral replication complexes (VRCs) from cellular nucleases and host defenses (Schwartz et al., 2002(Schwartz et al., , 2004Ding et al., 2004). Specifically, the replication complexes of plant viruses belonging to the genera Potyvirus, Comovirus, Dianthovirus, Pecluvirus, and Bromovirus cause proliferation and vesiculation of either the perinuclear or the cortical ER (Schaad et al., 1997;Dunoyer et al., 2002;Lee and Ahlquist, 2003). The replicases of cowpea mosaic virus and red clover necrotic mosaic virus induce ER proliferation (Carette et al., 2002a(Carette et al., , 2002bTurner et al., 2004). The best-studied example is the brome mosaic virus (BMV) 1a replicase, which localizes to the ER and induces membrane i...

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confidence: 97%

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The Potato Virus X TGBp2 Movement Protein Associates with Endoplasmic Reticulum-Derived Vesicles during Virus Infection

et al. 2005

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“…In regard to host factors, cytoskeletal elements have been implicated in assisting the movement of some plant viruses (Reichel and Beachy, 1999;Aaziz et al, 2001;Heinlein, 2002;Roberts and Oparka, 2003;Heinlein and Epel, 2004;Oparka, 2004;Waigmann et al, 2004;Nelson, 2005). During TMV infection, microtubules (MTs) and the viral MP colocalize in infected cells (McLean et al, 1995;Heinlein et al, 1995Heinlein et al, , 1998Boyko et al, 2000b).…”

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The Tobacco Mosaic Virus 126-Kilodalton Protein, a Constituent of the Virus Replication Complex, Alone or within the Complex Aligns with and Traffics along Microfilaments

2005

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Virus-induced cytoplasmic inclusion bodies (referred to as virus replication complexes [VRCs]) consisting of virus and host components are observed in plant cells infected with tobacco mosaic virus, but the components that modulate their form and function are not fully understood. Here, we show that the tobacco mosaic virus 126-kD protein fused with green fluorescent protein formed cytoplasmic bodies (126-bodies) in the absence of other viral components. Using mutant 126-kD:green fluorescent fusion proteins and viral constructs expressing the corresponding mutant 126-kD proteins, it was determined that the size of the 126-bodies and the corresponding VRCs changed in synchrony for each 126-kD protein mutation tested. Through colabeling experiments, we observed the coalignment and intracellular trafficking of 126-bodies and, regardless of size, VRCs, along microfilaments (MFs). Disruption of MFs with MF-depolymerizing agents or through virus-induced gene silencing compromised the intracellular trafficking of the 126-bodies and VRCs and virus cell-to-cell movement, but did not decrease virus accumulation to levels that would affect virus movement or prevent VRC formation. Our results indicate that (1) the 126-kD protein modulates VRC size and traffics along MFs in cells; (2) VRCs traffic along MFs in cells, possibly through an interaction with the 126-kD protein, and the negative effect of MF antagonists on 126-body and VRC intracellular movement and virus cellto-cell movement correlates with the disruption of this association; and (3) virus movement was not correlated with VRC size.

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“…This resemblance indicates physical and functional similarities between MPs and movement-associated proteins of potexviruses and tobamoviruses, suggesting that both viral groups utilize a similar method of intracellular movement, at least through a portion of this passage (Nelson, 2005).…”

Section: Intracellular and Intercellular Movementmentioning

confidence: 82%