Cell wall localization of Red clover necrotic mosaic virus movement protein is required for cell-to-cell movement

Cell–to–cell movement of tobacco mosaic virus (TMV) is used to illustrate macromolecular traffic through plant intercellular connections, the plasmodesmata. This transport process is mediated by a specialized viral movement protein, P30. In the initially infected cell, P30 is produced by transcription of a subgenomic RNA derived from the invading virus. Presumably, P30 then associates with a certain proportion of the viral RNA molecules, sequestering them from replication and mediating their transport into neighbouring uninfected host cells. This nucleoprotein complex is targeted to plasmodesmata, possibly via interaction with the host cell cytoskeleton. Prior to passage through a plasmodesma, the plasmodesmal channel is dilated by the movement protein. It is proposed that targeting of P30–TMV RNA complexes to plasmodesmata involves binding to a specific cell wall–associated receptor molecule. In addition, a cell wall–associated protein kinase, phosphorylates P30 at its carboxy–terminus and minimizes P30–induced interference with plasmodesmatal permeability during viral infection.

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Interference with initial and short-distance cell-to-cell movement of Tomato mosaic virus in transgenic tobacco plants with high expression of BcKELP, a virus movement protein interactor from Brassica campestris

Physiological and Molecular Plant Pathology ◽

10.1016/j.pmpp.2012.01.003 ◽

2012 ◽

Vol 78 ◽

pp. 38-44 ◽

Cited By ~ 4

Author(s):

Nobumitsu Sasaki ◽

Tatsuro Odawara ◽

Shoko Nagai ◽

Kazuma Yoshimura ◽

Yasuhiko Matsushita ◽

...

Keyword(s):

Mosaic Virus ◽

Transgenic Tobacco ◽

Short Distance ◽

Brassica Campestris ◽

Movement Protein ◽

Cell Movement ◽

Tomato Mosaic Virus ◽

Virus Movement ◽

Transgenic Tobacco Plants ◽

Tobacco Plants

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Mimicking carboxyterminal phosphorylation differentially effects subcellular distribution and cell-to-cell movement of Tobacco mosaic virus movement protein

Virology ◽

10.1016/j.virol.2004.11.040 ◽

2005 ◽

Vol 332 (2) ◽

pp. 563-577 ◽

Cited By ~ 32

Author(s):

Kateryna Trutnyeva ◽

Radostina Bachmaier ◽

Elisabeth Waigmann

Keyword(s):

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Subcellular Distribution ◽

Movement Protein ◽

Cell Movement ◽

Virus Movement

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Dysfunctionality of a tobacco mosaic virus movement protein mutant mimicking threonine 104 phosphorylation

Journal of General Virology ◽

10.1099/vir.0.18972-0 ◽

2003 ◽

Vol 84 (3) ◽

pp. 727-732 ◽

Cited By ~ 23

Author(s):

E. M. Karger ◽

O. Yu. Frolova ◽

N. V. Fedorova ◽

L. A. Baratova ◽

T. V. Ovchinnikova ◽

...

Keyword(s):

Endoplasmic Reticulum ◽

Tobacco Mosaic Virus ◽

Mosaic Virus ◽

Movement Protein ◽

Cell Movement ◽

Specific Protein ◽

Virus Movement ◽

Wild Type ◽

Molecular Masses

Replication of tobacco mosaic virus (TMV) is connected with endoplasmic reticulum (ER)-associated membranes at early stages of infection. This study reports that TMV movement protein (MP)-specific protein kinases (PKs) associated with the ER of tobacco were capable of phosphorylating Thr104 in TMV MP. The MP-specific PKs with apparent molecular masses of about 45–50 kDa and 38 kDa were revealed by gel PK assays. Two types of mutations were introduced in TMV MP gene of wild-type TMV U1 genome to substitute Thr104 by neutral Ala or by negatively charged Asp. Mutation of Thr104 to Ala did not affect the size of necrotic lesions induced by the mutant virus in Nicotiana tabacum Xanthi nc. plants. Conversely, mutation of Thr to Asp mimicking Thr104 phosphorylation strongly inhibited cell-to-cell movement. The possible role of Thr104 phosphorylation in TMV MP function is discussed.

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