Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during Infection (original) (raw)
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aDivision of Plant Biology, BCC 206, Department of Cell Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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aDivision of Plant Biology, BCC 206, Department of Cell Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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bBiology Department, Washington University, St. Louis, Missouri 63130-4899
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bBiology Department, Washington University, St. Louis, Missouri 63130-4899
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aDivision of Plant Biology, BCC 206, Department of Cell Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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cDepartment of Plant Sciences, Tel Aviv University, Tel Aviv 69978, Israel
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aDivision of Plant Biology, BCC 206, Department of Cell Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, California 92037
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Received:
23 February 1998
Cite
Manfred Heinlein, Hal S. Padgett, J. Scott Gens, Barbara G. Pickard, Steven J. Casper, Bernard L. Epel, Roger N. Beachy, Changing Patterns of Localization of the Tobacco Mosaic Virus Movement Protein and Replicase to the Endoplasmic Reticulum and Microtubules during Infection, The Plant Cell, Volume 10, Issue 7, July 1998, Pages 1107–1120, https://doi.org/10.1105/tpc.10.7.1107
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Abstract
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.
© 1998 American Society of Plant Physiologists
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