Some ultrastructural and cytochemical observations on Chinese cabbage leaves infected with cauliflower mosaic virus

Conti, Giovanni Maria; Vegetti, G.; Bassi, Maria; Favali, M. A.

doi:10.1016/0042-6822(72)90559-4

Cited by 55 publications

(21 citation statements)

References 15 publications

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“…7B). These findings are in agreement with those from earlier work, in which electron micrographs showed the protrusion of CaMV tubules into the cytoplasm (Conti et al, 1972). Furthermore, the tubules formed from the CaMV MP are similar in structure and orientation to those produced by the GFLV MP (Amari et al, 2010).…”

Section: Atsrc22 Localizes To the Plasma Membrane And Colocalizes Wisupporting

confidence: 93%

“…Most electron micrographs of P6 IBs show a single, very large, amorphous IB in the cell, with individual virions embedded in the matrix (Fujisawa et al, 1967;Conti et al, 1972). Electron microscopy has also shown that CaMV moves from cell to cell as virions through tubules (Conti et al, 1972;Stavolone et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

“…The CaMV MP forms tubules that project through plasmodesmata, which are then used for transport of the icosahedral virions from cell to cell (Perbal et al, 1993;Kasteel et al, 1996;Benitez-Alfonso et al, 2010). Tubules were reported in plant tissues infected with CaMV in early studies (Conti et al, 1972). Similar tubule structures are produced in plant protoplasts and insect cells after the introduction and expression of the CaMV MP (Kasteel et al, 1996;Huang et al, 2000).…”

Section: Atsrc22 Localizes To the Plasma Membrane And Colocalizes Wimentioning

confidence: 91%

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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: Atsrc22 Localizes To the Plasma Membrane And Colocalizes Wisupporting

confidence: 93%

Section: Discussionmentioning

confidence: 99%

Section: Atsrc22 Localizes To the Plasma Membrane And Colocalizes Wimentioning

confidence: 91%

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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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“…Van der Scheer & Groenewegen, 1971;Kim & Fulton, 1971Kim, 1979); nepoviruses (e.g. Roberts & Harrison, 1970;Jones et al, 1973;Hibino et al, 1977;Di Franco et al, 1983) and caulimoviruses (Kitajima & Lauritis, 1969;Conti et al., 1972;Linstead et al, 1988) also induce tubules. However, this is the first report on the formation of these structures in infected protoplasts, i.e.…”

Section: Discussionmentioning

confidence: 99%

Tubular structures involved in movement of cowpea mosaic virus are also formed in infected cowpea protoplasts

Lent¹,

Storms²,

Meer³

et al. 1991

Journal of General Virology

167

104

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In cowpea plant cells infected with cowpea mosaic virus, tubular structures containing virus particles are formed in the plasmodesmata between adjacent cells; these structures are supposedly involved in cell-to-cell spread of the virus. Here we show that similar tubular structures are also formed in cowpea protoplasts, from which the cell wall and plasmodesmata are absent. Between 12 and 21 h post-inoculation, tubule formation starts in the periphery of the protoplast at the level of the plasma membrane. Upon assembly, the viruscontaining tubule is enveloped by the plasma membrane and extends into the culture medium. This suggests that the tubule has functional polarity and makes it likely that a tubule 'grows' into a neighbouring cell in vivo. On average, 75 % of infected protoplasts were shown to possess tubular structures extending from their surface. The tubule wall was 3 to 4 nm thick and they were up to 20 gm in length, as shown by fluorescent light microscopy and negative staining electron microscopy. By analogy to infected plant cells, both the viral 58K/48K movement and capsid proteins were located in these tubules, as determined by immunofluorescent staining and immunogold labelling using specific antisera against these proteins. These results demonstrate that the formation of tubules is not necessarily dependent on the presence of plasmodesmata or the cell wall, and that they are composed, at least in part, of virus-encoded components.

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“…They are maize rough dwarf (Gerola & Bassi, 1966), dahlia mosaic (Kitajima & Lauritis,I969), bean pod mottle (Kim & Fulton, 1970, cowpea mosaic (Van der Scheer & Groenewegen, I97I), radish mosaic (Honda & Matsui,I972), cauliflower mosaic (Conti et al 1972 ) and carrot mottle (Murant & Roberts,197o) viruses. The significance of these protrusions is, however, not known.…”

Section: Ultrastructural Changes In Differentiated Leaf Cellsmentioning

confidence: 99%

Ultrastructural Changes in Differentiated Leaf Cells Infected with Cherry Leaf Roll Virus

Jones

Kinninmonth

Roberts

1973

Journal of General Virology

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Some ultrastructural and cytochemical observations on Chinese cabbage leaves infected with cauliflower mosaic virus

Cited by 55 publications

References 15 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

Tubular structures involved in movement of cowpea mosaic virus are also formed in infected cowpea protoplasts

Ultrastructural Changes in Differentiated Leaf Cells Infected with Cherry Leaf Roll Virus

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