The cowpea mosaic virus M RNA-encoded 48-kilodalton protein is responsible for induction of tubular structures in protoplasts

Wellink, J.; Lent, J.W.M. van; Verver, J.; Sijen, Titia; Goldbach, Rob; Kammen, A. B. Van

doi:10.1128/jvi.67.6.3660-3664.1993

Cited by 83 publications

(27 citation statements)

References 17 publications

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“…The appearance of MP:GFP plasma membrane protrusions is reminiscent of the projections on the surface of plant protoplasts and insect cells that express the movement proteins of tubule-forming viruses such as cowpea mosaic virus (van Lent et al, 1991;Wellink et al, 1993;Kasteel et al, 1996), cauliflower mosaic virus (Perbal et al, 1993;Kasteel et al, 1996), tomato spotted wilt virus (Storms et al, 1995), and grapevine fanleaf nepovirus (Ritzenthaler et al, 1995). In contrast to TMV, these viruses apparently move between cells as virions through such tubules.…”

Section: Discussionmentioning

confidence: 99%

Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during Infection

Heinlein¹,

Padgett²,

Gens³

et al. 1998

The Plant Cell

161

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Tobacco mosaic virus (TMV) derivatives that encode movement protein (MP) as a fusion to the green fluorescent protein (MP:GFP) were used in combination with antibody staining to identify host cell components to which MP and replicase accumulate in cells of infected Nicotiana benthamiana leaves and in infected BY-2 protoplasts. MP:GFP and replicase colocalized to the endoplasmic reticulum (ER; especially the cortical ER) and were present in large, irregularly shaped, ER-derived structures that may represent "viral factories." The ER-derived structures required an intact cytoskeleton, and microtubules appeared to redistribute MP:GFP from these sites during late stages of infection. In leaves, MP:GFP accumulated in plasmodesmata, whereas in protoplasts, the MP:GFP was targeted to distinct, punctate sites near the plasma membrane. Treating protoplasts with cytochalasin D and brefeldin A at the time of inoculation prevented the accumulation of MP:GFP at these sites. It is proposed that the punctate sites anchor the cortical ER to plasma membrane and are related to sites at which plasmodesmata form in walled cells. Hairlike structures containing MP:GFP appeared on the surface of some of the infected protoplasts and are reminiscent of similar structures induced by other plant viruses. We present a model that postulates the role of the ER and cytoskeleton in targeting the MP and viral ribonucleoprotein from sites of virus synthesis to the plasmodesmata through which infection is spread.

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Section: Discussionmentioning

confidence: 99%

Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during Infection

Heinlein¹,

Padgett²,

Gens³

et al. 1998

The Plant Cell

161

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“…These structures exhibit many of the features of tubules visualized in plants in that they contain MP and, in the case of infected protoplasts, are filled with virus particles. Mature virions, however, are not required for CPMV tubuleformation (Kasteel et al, 1993;Wellink et al, 1993). The protoplast data clearly indicate that plasmodesmata are unnecessary for most aspects of tubule development, but it is certainly possible that a plasmodesmal channel provides an opening to initiate tubule extension in intact tissue.…”

Section: Lntercellular Transport Of Genomes Through Plasmodesmata-tmvmentioning

confidence: 97%

“…A striking feature of the CPMV, CaMV, and tomato spotted wilt tospovirus MPs is their ability to induce tubules in protoplasts and cultured insect cells. In both cell systems, expression of MP results in tubular protrusions of up to 50 pm in length extending from the cell surface (van Lent et al, 1991;Kasteel et al, 1993Kasteel et al, , 1996Perbal et al, 1993;Wellink et al, 1993;Storms et al, 1995). The plasma membrane is contiguous with the exterior of the tubules.…”

Section: Lntercellular Transport Of Genomes Through Plasmodesmata-tmvmentioning

confidence: 99%

Cell-to-Cell and Long-Distance Transport of Viruses in Plants

Carrington¹,

Kasschau²,

Mahajan³

et al. 1996

The Plant Cell

340

314

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“…Ophiovirus particles have been described as open circular CP-decorated flexuous filaments with a thickness of 3 to 4 nm (55). Since tubule-forming viruses usually have an icosahedral particle morphology, such as CPMV (15,37), CaMV (11,27,32,33), GFLV (27,(34)(35)(36), alfalfa mosaic virus, brome mosaic virus (39), and tomato spotted wild virus (13), the use of a tubule-guided mechanism by CPsV may be unexpected. Tubule-guided movement by icosahedral viruses depends on CP-MP interactions that may allow the viral particles to be guided along the inner tubule wall (56)(57)(58)(59).…”

Section: Discussionmentioning

confidence: 99%

“…PDLPs require the ER-Golgi pathway for their targeting to PD (27,29), which may explain the observed sensitivity of tubule formation and tubule-mediated virus movement to secretory pathway inhibitors (27,30,31). DNA and RNA viruses that move from cell to cell by a tubule-guided mechanism have been found in the Caulimoviridae (11,27,32,33), Secoviridae (15,27,(34)(35)(36)(37), Bunyaviridae (13,38), and Bromoviridae (39) families.…”

mentioning

confidence: 99%

Citrus Psorosis Virus Movement Protein Contains an Aspartic Protease Required for Autocleavage and the Formation of Tubule-Like Structures at Plasmodesmata

Luna

Peña

Borniego

et al. 2018

J Virol

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Plant virus cell-to-cell movement is an essential step in viral infections. This process is facilitated by specific virus-encoded movement proteins (MPs), which manipulate the cell wall channels between neighboring cells known as plasmodesmata (PD). Citrus psorosis virus (CPsV) infection in sweet orange involves the formation of tubule-like structures within PD, suggesting that CPsV belongs to "tubule-forming" viruses that encode MPs able to assemble a hollow tubule extending between cells to allow virus movement. Consistent with this hypothesis, we show that the MP of CPsV (MP) indeed forms tubule-like structures at PD upon transient expression in leaves. Tubule formation by MP depends on its cleavage capacity, mediated by a specific aspartic protease motif present in its primary sequence. A single amino acid mutation in this motif abolishes MP cleavage, alters the subcellular localization of the protein, and negatively affects its activity in facilitating virus movement. The amino-terminal 34-kDa cleavage product (34K), but not the 20-kDa fragment (20K), supports virus movement. Moreover, similar to tubule-forming MPs of other viruses, MP (and also the 34K cleavage product) can homooligomerize, interact with PD-located protein 1 (PDLP1), and assemble tubule-like structures at PD by a mechanism dependent on the secretory pathway. 20K retains the protease activity and is able to cleave a cleavage-deficient MP in Altogether, these results demonstrate that CPsV movement depends on the autolytic cleavage of MP by an aspartic protease activity, which removes the 20K protease and thereby releases the 34K protein for PDLP1-dependent tubule formation at PD. Infection by citrus psorosis virus (CPsV) involves a self-cleaving aspartic protease activity within the viral movement protein (MP), which results in the production of two peptides, termed 34K and 20K, that carry the MP and viral protease activities, respectively. The underlying protease motif within the MP is also found in the MPs of other members of the family, suggesting that protease-mediated protein processing represents a conserved mechanism of protein expression in this virus family. The results also demonstrate that CPsV and potentially other ophioviruses move by a tubule-guided mechanism. Although several viruses from different genera were shown to use this mechanism for cell-to-cell movement, our results also demonstrate that this mechanism is controlled by posttranslational protein cleavage. Moreover, given that tubule formation and virus movement could be inhibited by a mutation in the protease motif, targeting the protease activity for inactivation could represent an important approach for ophiovirus control.

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The cowpea mosaic virus M RNA-encoded 48-kilodalton protein is responsible for induction of tubular structures in protoplasts

Cited by 83 publications

References 17 publications

Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during Infection

Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during Infection

Cell-to-Cell and Long-Distance Transport of Viruses in Plants

Citrus Psorosis Virus Movement Protein Contains an Aspartic Protease Required for Autocleavage and the Formation of Tubule-Like Structures at Plasmodesmata

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