PLPA 652/BIOPL 652 Molecular Plant Pathology

Virus Movement

4 February 2002 S. Lazarowitz

 

A.   Virus movement proteins coordinate viral genome replication with its directed movement within and between cells

1.   Models for virus movement: overview of TMV, SqLCV, ‘tubule’ viruses, PVX (Lazarowitz and Beachy, 1999).

B.   TMV: a model for cytoskeletal trafficking, and plasmodesmal targeting and gating.

1.   30 kD protein as an RNA binding protein (Citovsky et al., 1990; Citovsky et al., 1992).

2.   30 kD protein (and other MPs) effects size exclusion limits of PD (Ding et al., 1992; Fujiwara et al., 1993; Oparka et al., 1997; Waigmann et al., 1994; Wolf et al., 1989).

a.       Microinjection vs. in vivo expression of GFP-MP alone and during infection:  what each can and cannot tell you (Oparka et al., 1997; Oparka et al., 1999).

b.       Proteins as large as 50 kD can move through PD in sink leaves! (Oparka et al., 1999).

3.            Associations with actin filaments and microtubules (Heinlein et al., 1995; Heinlein et al., 1998; McLean et al., 1995; Reichel and Beachy, 1998).

4.   The 30 kD MP interacts with a cell wall pectin methylesterase (Chen et al., 2000).

C.   SqLCV: a model for nuclear shuttling, directional movement, and biogenesis of cell wall channels.

1.   NSP is a ssDNA binding protein (Pascal et al., 1994).

2.   Subcellular localization of NSP and MPB: nuclear and ER targeting, tubules as potential analog of the PD desmotubule (Pascal et al., 1994; Ward et al., 1997).

3.   Cooperative interaction of MPs and nuclear shuttling shown in living plant cells (Sanderfoot et al., 1996; Sanderfoot and Lazarowitz, 1995).

4.   Identification of a plant nuclear export signal (Ward and Lazarowitz, 1999).

D.   PVX: insights into systemic movement.

1.       Virus particles move cell-to-cell: requirements for CP and ‘triple gene block’ MPs (Angell and Baulcombe, 1995; Angell et al., 1996; Hefferon et al., 1997; Kalinina et al., 1996; Oparka et al., 1996; Santa Cruz et al., 1996; Santa Cruz et al., 1998). 

2.       CP and smaller two TGB MPs (12K, 8K) interact and modulate function of the largest TGB MP (25K) (Yang et al., 2000).

2.   CP is required for systemic movement (Santa Cruz et al., 1998). 

3.   Exiting phloem companion cells and entering sieve elements:  disassembling and reassembling (Santa Cruz et al., 1998)?

 

References

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Angell, S. M., Davies, C., and Baulcombe, D. C. (1996). Cell-to-cell movement of potato virus X is associated with a change in the size-exclusion limit of plasmodesmata in trichome cells of Nicotiana clevelandii. Virology 216: 197-201.

Chen, M. H., Sheng, J., Hind, G., Handa, A. K. and Citovsky, V. (2000). Interaction between the tobacco mosaic virus movement protein and host cell pectin methylesterases is required for viral cell-to-cell movement.  EMBO J 13: 913-920.

Citovsky, V., Knorr, D., Schuster, G., and Zambryski, P. (1990). The P30 movement protein of tobacco mosaic virus is a single-stranded nucleic acid binding protein. Cell 60: 637-647.

Citovsky, V., Wong, M. L., Shaw, A. L., Venkataram Prasad, B. V., and Zambryski, P. (1992). Visualization and characterization of tobacco mosaic virus movement protein binding to single-stranded nucleic acids. Plant Cell 4: 397-411.

Ding, B., Haudenshield, J. S., Hull, R. J., Wolf, S., Beachy, R. N., and Lucas, W. J. (1992). Secondary plasmodesmata are specific sites of localization of the tobacco mosaic virus movement protein in transgenic tobacco plants. The Plant Cell 4: 915-928.

Fujiwara, T., Giesman-Cookmeyer, D., Ding, B., Lommel, S. A., and Lucas, W. J. (1993). Cell-to-cell trafficking of macromolecules through plasmodesmata potentiated by the red clover necrotic virus movement protein. Plant Cell 5: 1783-1794.

Hefferon, K. L., Doyle, S., and AbouHaidar, M. G. (1997). Immunological detection of the 8K protein of potato virus X (PVX) in cell walls of PVX-infected tobacco and transgenic potato. Arch Virol 142: 425-33.

Heinlein, M., Epel, B. L., Padgett, H. S., and Beachy, R. N. (1995). Interaction of Tobamovirus Movement Proteins With the Plant Cytoskeleton. Science 270: 1983-1985.

Heinlein, M., Padgett, H. S., Gens, J. S., Pickard, B. G., Casper, S. J., Epel, B. L., and Beachy, R. N. (1998). Changing patterns of localization of the tobacco mosaic virus movement protein and replicase to the endoplasmic reticulum and microtubules during infection. Plant Cell 10: 1107-1120.

Kalinina, N. O., Fedorkin, O. N., Samuilova, O. V., Maiss, E., Korpela, T., Morozov, S., and Atabekov, J. G. (1996). Expression and biochemical analyses of the recombinant potato virus X 25K movement protein. FEBS Lett 397: 75-8.

Lazarowitz, S. G., and Beachy, R. N. (1999). Viral movement proteins as probes for investigating intracellular and intercellular trafficking in plants. Plant Cell 11: 535-548.

McLean, B. G., Zupan, J., and Zambryski, P. C. (1995). Tobacco mosiac virus movement protein associates with the cytoskeleton in tobacco cells. Plant Cell 7: 2101-2114.

Oparka, K. J., Prior, D. A., Santa Cruz, S., Padgett, H. S., and Beachy, R. N. (1997). Gating of epidermal plasmodesmata is restricted to the leading edge of expanding infection sites of tobacco mosaic virus (TMV). Plant J 12: 781-789.

Oparka, K. J., Prior, D. A. M., SantaCruz, S., Padgett, H. S., and Beachy, R. N. (1997). Gating of epidermal plasmodesmata is restricted to the leading edge of expanding infection sites of tobacco mosaic virus (TMV). Plant Journal 12: 781-789.

Oparka, K. J., Roberts, A. G., Boevink, P., Santa Cruz, S., Roberts, I., Pradel, K. S., Imlau, A., Kotlizky, G., Sauer, N., Epel, B., and Turgeon, R. (1999). Simple, but not branched, plasmodesmata allow the nonspecific trafficking of proteins in developing tobacco leaves.  Cell 97: 743-54.

Oparka, K. J., Roberts, A. G., Roberts, I. M., Prior, D. A. M., and SantaCruz, S. (1996). Viral coat protein is targeted to, but does not gate, plasmodesmata during cell-to-cell movement of potato virus X. Plant Journal 10: 805-813.

Oparka, K. J., Roberts, A. G., Boevink, P. et al. (1999). Simple, but not branched, plasmodesmata allow the nonspecific trafficking of proteins in developing tobacco leaves  Cell 97: 743-754.

Pascal, E., Sanderfoot, A. A., Ward, B. M., Medville, R., Turgeon, R., and Lazarowitz, S. G. (1994). The geminivirus BR1 movement protein binds single-stranded DNA and localizes to the cell nucleus. Plant Cell 6: 995-1006.

Reichel, C., and Beachy, R. N. (1998). Tobacco mosaic virus infection induces severe morphological changes of the endoplasmic reticulum. Proc. Natl. Acad. Sci. USA 95: 11169-11174.

Sanderfoot, A. A., Ingham, D. J., and Lazarowitz, S. G. (1996). A viral movement protein as a nuclear shuttle:  The geminivirus BR1 movement protein contains domains essential for interaction with BL1 and nuclear localization. Plant Physiol. 110: 23-33.

Sanderfoot, A. A., and Lazarowitz, S. G. (1995). Cooperation in viral movement: the geminivirus BL1 movement protein interacts with BR1 and redirects it from the nucleus to the cell periphery. Plant Cell 7: 1185-1194.

Santa Cruz, S., Chapman, S., Roberts, A. G., Roberts, I. M., Prior, D. A. M., and Oparka, K. J. (1996). Assembly and movement of a plant virus carrying a green fluorescent protein overcoat. Proc. Natl. Acad. Sci. 93: 6286-6290.

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Ward, B. M., and Lazarowitz, S. G. (1999). Nuclear export in plants:  Use of geminivirus movement proteins for an in vivo cell based export assay. Plant Cell 11: in press.

Ward, B. M., Medville, R., Lazarowitz, S. G., and Turgeon, R. (1997). The geminivirus BL1 movement protein is associated with endoplasmic reticulum-derived tubules in developing phloem cells. J. Virology 71: 3726-3733.

Wolf, S., Deom, C. M., Beachy, R. N., and Lucas, W. J. (1989). Movement protein of tobacco mosaic virus modifies plasmodesmatal size exclusion limit.  Science 246: 377-379.

Yang, Y., Ding, B., Baulcombe, D.C. and Verchot, J. (2000).  Cell-to-cell movement of the 25K protein of potato virus X is regulated by three other viral proteins. MPMI 13:599-605.