scholarly journals Alfalfa Mosaic Virus Movement Protein Induces Tubules in Plant Protoplasts

1997 ◽  
Vol 10 (8) ◽  
pp. 1010-1014 ◽  
Author(s):  
Huanquan Zheng ◽  
Guiling Wang ◽  
Lee Zhang
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Green Fluorescence Protein ◽  
Virus Movement ◽  
Plant Protoplasts ◽  
Tubular Structures ◽  
Green Fluorescence ◽  
Tubule Formation ◽  
Fluorescence Protein

The alfalfa mosaic virus (AlMV) movement protein (MP) was fused with the green fluorescence protein (GFP). The MP-GFP fusion was transiently expressed in protoplasts prepared from Nicotiana tabacum, resulting in the production of long, extending, tubular structures protruding from the protoplast surface. Deletions of MP amino acids 1 to 77, 84 to 142, or 226 to 300 all affected tubule formation. Hence, the AlMV MP is solely required for the induction of the tubular structures, and the results suggest that AlMV may move from cell to cell via tubules.

scholarly journals Effects of Movement Protein Mutations on the Formation of Tubules in Plant Protoplasts Expressing a Fusion Between the Green Fluorescent Protein and Cauliflower mosaic virus Movement Protein

2001 ◽  
Vol 14 (8) ◽  
pp. 1026-1031 ◽  
Author(s):  
Zhong Huang ◽  
Yu Han ◽  
Stephen H. Howell
Keyword(s):  
Green Fluorescent Protein ◽  
Mosaic Virus ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Cauliflower Mosaic Virus ◽  
Virus Movement ◽  
Plant Protoplasts ◽  
Tubule Formation ◽  
Leaf Mesophyll ◽  
Green Fluorescent

Fusions between the green fluorescent protein (GFP) and the Cauliflower mosaic virus (CaMV) movement protein (MP) induce the formation of fluorescent foci and surface tubules in Arabidopsis thaliana leaf mesophyll protoplasts. Tubules elongate coordinately and progressively in an assembly process approximately 6 to 12 h following transfection of protoplasts with GFP-MP constructs. Tubules are not formed in protoplasts transfected by GFP-MPER2A, a MP mutation that renders CaMV noninfectious. A small number of short tubules are formed on protoplasts transfected by GFP-MPN6 and GFP-MPN13, two second-site revertants of ER2A that partially restore infectivity. Protoplasts cotransfected with cyan fluorescent protein (CFP)-MPWT and GFP-MPER2A form tubules containing both MP fusions, indicating that although the GFP-MPER2A cannot induce tubule formation, GFP-MPER2A can coassemble or colocalize with CFP-MPWT in tubules. Thus, CaMV MP-induced tubule formation in protoplasts correlates closely with the infectivity of mutation ER2A and its revertants, suggesting that tubule-forming capacity in plant protoplasts reflects a process required for virus infection or movement.

Limitations on the use of fused green fluorescent protein to investigate structure–function relationships for the cauliflower mosaic virus movement protein

Microbiology ◽  
2000 ◽  
Vol 81 (7) ◽  
pp. 1851-1855 ◽  
Author(s):  
Carole L. Thomas ◽  
Andrew J. Maule
Keyword(s):  
Green Fluorescent Protein ◽  
Mosaic Virus ◽  
Fluorescent Protein ◽  
Movement Protein ◽  
Cauliflower Mosaic Virus ◽  
Virus Movement ◽  
Wild Type ◽  
Tubule Formation ◽  
Mouth Disease Virus ◽  
Green Fluorescent

To investigate the process of tubule formation for the cauliflower mosaic virus movement protein (CaMV MP), the green fluorescent protein (GFP) was fused to the MP to provide a vital marker for MP location after expression in insect cells. In contrast to the long tubular structures seen previously following baculovirus-based expression of the wild-type MP, the fusion protein produced only aggregates of fluorescing material in the cytoplasm. However, by co-expressing wild-type MP and GFP–MP, or by engineering their co-accumulation by introducing a foot-and-mouth disease virus 2A cleavage sequence between GFP and MP, long GFP-fluorescing tubules were formed. The experiments suggest that the presence of GFP at the N or C terminus of the tubule-forming domain of the CaMV MP places steric constraints upon the aggregation of the MP into a tubule but that this can be overcome by providing wild-type protein for inclusion in the aggregate.

scholarly journals Systemic transport of Alfalfa mosaic virus can be mediated by the movement proteins of several viruses assigned to five genera of the 30K family

2013 ◽  
Vol 94 (3) ◽  
pp. 677-681 ◽  
Author(s):  
Thor V. M. Fajardo ◽  
Ana Peiró ◽  
Vicente Pallás ◽  
Jesús Sánchez-Navarro
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Brome Mosaic Virus ◽  
Virus Movement ◽  
Cell Transport ◽  
Movement Proteins ◽  
C Terminus ◽  
Prunus Necrotic Ringspot Virus ◽  
Systemic Transport

We previously showed that the movement protein (MP) gene of Alfalfa mosaic virus (AMV) is functionally exchangeable for the cell-to-cell transport of the corresponding genes of Tobacco mosaic virus (TMV), Brome mosaic virus, Prunus necrotic ringspot virus, Cucumber mosaic virus and Cowpea mosaic virus. We have analysed the capacity of the heterologous MPs to systemically transport the corresponding chimeric AMV genome. All MPs were competent in systemic transport but required the fusion at their C terminus of the coat protein-interacting C-terminal 44 aa (A44) of the AMV MP. Except for the TMV MP, the presence of the hybrid virus in upper leaves correlated with the capacity to move locally. These results suggest that all the MPs assigned to the 30K superfamily should be exchangeable not only for local virus movement but also for systemic transport when the A44 fragment is present.

Nucleic acid-binding properties of the alfalfa mosaic virus movement protein produced in yeast

Virology ◽  
1992 ◽  
Vol 188 (2) ◽  
pp. 896-899 ◽  
Author(s):  
Fabrice Schoumacher ◽  
Claude Erny ◽  
Anne Berna ◽  
Therese Godefroy-Colburn ◽  
Christiane Stussi-Garaud
Keyword(s):  
Nucleic Acid ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Virus Movement ◽  
Nucleic Acid Binding ◽  
Binding Properties

scholarly journals Intracellular Localization and Movement Phenotypes of Alfalfa mosaic virus Movement Protein Mutants

2001 ◽  
Vol 14 (9) ◽  
pp. 1063-1074 ◽  
Author(s):  
Mei Huang ◽  
Laurian Jongejan ◽  
Huanquan Zheng ◽  
Lee Zhang ◽  
John F. Bol
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Intracellular Localization ◽  
Alfalfa Mosaic Virus ◽  
Epidermal Cells ◽  
Tissue Cell ◽  
Tubular Structures ◽  
Suspension Cells ◽  
Long Distance ◽  
Tobacco Suspension Cells

Thirteen mutations were introduced in the movement protein (MP) gene of Alfalfa mosaic virus (AMV) fused to the green fluorescent protein (GFP) gene and the mutant MP-GFP fusions were expressed transiently in tobacco protoplasts, tobacco suspension cells, and epidermal cells of tobacco leaves. In addition, the mutations were introduced in the MP gene of AMV RNA 3 and the mutant RNAs were used to infect tobacco plants. Ten mutants were affected in one or more of the following functions of MP: the formation of tubular structures on the surface of protoplasts, association with the endoplasmic reticulum (ER) of suspension cells and epidermal cells, targeting to punctate structures in the cell wall of epidermis cells, movement from transfected cells to adjacent cells in epidermis tissue, cell-to-cell movement, or long-distance movement in plants. The mutations point to functional domains of the MP and support the proposed order of events in AMV transport. Studies with several inhibitors indicate that actin or microtubule components of the cytoskeleton are not involved in tubule formation by AMV MP. Evidence was obtained that tubular structures on the surface of transfected protoplasts contain ER- or plasmalemma-derived material.

scholarly journals Effect of the alfalfa mosaic virus movement protein expressed in transgenic plants on the permeability of plasmodesmata

1993 ◽  
Vol 74 (11) ◽  
pp. 2459-2461 ◽  
Author(s):  
A. Poirson ◽  
A. P. Turner ◽  
C. Giovane ◽  
A. Berna ◽  
K. Roberts ◽  
...  
Keyword(s):  
Transgenic Plants ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Virus Movement

scholarly journals An N-proximal sequence of the alfalfa mosaic virus movement protein is necessary for association with cell walls in transgenic plants

1992 ◽  
Vol 73 (8) ◽  
pp. 2115-2119 ◽  
Author(s):  
C. Erny ◽  
F. Schoumacher ◽  
C. Jung ◽  
M.-J. Gagey ◽  
T. Godefroy-Colburn ◽  
...  
Keyword(s):  
Transgenic Plants ◽  
Mosaic Virus ◽  
Cell Walls ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Virus Movement

Phosphorylation of alfalfa mosaic virus movement protein in vivo

2014 ◽  
Vol 159 (7) ◽  
pp. 1787-1791 ◽  
Author(s):  
Bong-Suk Kim ◽  
Edward L. Halk ◽  
Donald J. Merlo ◽  
Steven E. Nelson ◽  
L. Sue Loesch-Fries
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Virus Movement

scholarly journals Binding of RNA by the alfalfa mosaic virus movement protein is biphasic

FEBS Letters ◽  
1992 ◽  
Vol 308 (3) ◽  
pp. 231-234 ◽  
Author(s):  
Fabrice Schoumacher ◽  
Marie-Josèphe Gagey ◽  
Michel Maira ◽  
Christiane Stussi-Garaud ◽  
Thérése Godefroy-Colburn
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Virus Movement

scholarly journals Mapping of the RNA-binding Domain of the Alfalfa Mosaic Virus Movement Protein

1994 ◽  
Vol 75 (11) ◽  
pp. 3199-3202 ◽  
Author(s):  
F. Schoumacher ◽  
C. Giovane ◽  
M. Maira ◽  
A. Poirson ◽  
T. Godefroy-Colburn ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Rna Binding ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Binding Domain ◽  
Virus Movement ◽  
Rna Binding Domain
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