Coat protein-independent cell-to-cell movement of bromoviruses expressing brome mosaic virus movement protein with an adaptation-related amino acid change in the central region

2005 ◽  
Vol 150 (6) ◽  
pp. 1231-1240 ◽  
Author(s):  
N. Sasaki ◽  
M. Kaido ◽  
T. Okuno ◽  
K. Mise
Keyword(s):  
Amino Acid ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Central Region ◽  
Amino Acid Change ◽  
Movement Protein ◽  
Cell Movement ◽  
Brome Mosaic Virus ◽  
Virus Movement ◽  
Related Amino Acid

scholarly journals Conversion in the Requirement of Coat Protein in Cell-to-Cell Movement Mediated by the Cucumber Mosaic Virus Movement Protein

2001 ◽  
Vol 75 (17) ◽  
pp. 8045-8053 ◽  
Author(s):  
Hideaki Nagano ◽  
Kazuyuki Mise ◽  
Iwao Furusawa ◽  
Tetsuro Okuno
Keyword(s):  
Amino Acids ◽  
Coat Protein ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Plant Viruses ◽  
Brome Mosaic Virus ◽  
Viral Movement ◽  
Intercellular Movement

ABSTRACT Plant viruses have movement protein (MP) gene(s) essential for cell-to-cell movement in hosts. Cucumber mosaic virus (CMV) requires its own coat protein (CP) in addition to the MP for intercellular movement. Our present results using variants of both CMV and a chimeric Brome mosaic virus with the CMV MP gene revealed that CMV MP truncated in its C-terminal 33 amino acids has the ability to mediate viral movement independently of CP. Coexpression of the intact and truncated CMV MPs extremely reduced movement of the chimeric viruses, suggesting that these heterogeneous CMV MPs function antagonistically. Sequential deletion analyses of the CMV MP revealed that the dispensability of CP occurred when the C-terminal deletion ranged between 31 and 36 amino acids and that shorter deletion impaired the ability of the MP to promote viral movement. This is the first report that a region of MP determines the requirement of CP in cell-to-cell movement of a plant virus.

scholarly journals Role of the Alfalfa mosaic virus Movement Protein and Coat Protein in Virus Transport

2001 ◽  
Vol 14 (9) ◽  
pp. 1051-1062 ◽  
Author(s):  
Jesús A. Sánchez-Navarro ◽  
John F. Bol
Keyword(s):  
Amino Acids ◽  
Coat Protein ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Alfalfa Mosaic Virus ◽  
Cell Movement ◽  
Brome Mosaic Virus ◽  
Tubular Structures ◽  
Wild Type ◽  
Virus Transport

The movement protein (MP) and coat protein (CP) encoded by Alfalfa mosaic virus (AMV) RNA 3 are both required for virus transport. RNA 3 vectors that expressed nonfused green fluorescent protein (GFP), MP:GPF fusions, or GFP:CP fusions were used to study the functioning of mutant MP and CP in protoplasts and plants. C-terminal deletions of up to 21 amino acids did not interfere with the function of the CP in cell-to-cell movement, although some of these mutations interfered with virion assembly. Deletion of the N-terminal 11 or C-terminal 45 amino acids did not interfere with the ability of MP to assemble into tubular structures on the protoplast surface. Additionally, N- or C-terminal deletions disrupted tubule formation. A GFP:CP fusion was targeted specifically into tubules consisting of a wild-type MP. All MP deletion mutants that showed cell-to-cell and systemic movement in plants were able to form tubular structures on the surface of protoplasts. Brome mosaic virus (BMV) MP did not support AMV transport. When the C-terminal 48 amino acids were replaced by the C-terminal 44 amino acids of the AMV MP, however, the BMV/AMV chimeric protein permitted wild-type levels of AMV transport. Apparently, the C terminus of the AMV MP, although dispensable for cell-to-cell movement, confers specificity to the transport process.

scholarly journals The C terminus of the movement protein of Brome mosaic virus controls the requirement for coat protein in cell-to-cell movement and plays a role in long-distance movement

2004 ◽  
Vol 85 (6) ◽  
pp. 1751-1761 ◽  
Author(s):  
Atsushi Takeda ◽  
Masanori Kaido ◽  
Tetsuro Okuno ◽  
Kazuyuki Mise
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Brome Mosaic Virus ◽  
Wild Type ◽  
Long Distance ◽  
C Terminus ◽  
Mouth Disease Virus ◽  
Long Distance Movement

The 3a movement protein (MP) plays a central role in the movement of Brome mosaic virus (BMV). To identify the functional regions in BMV MP, 24 alanine-scanning (AS) MP mutants of BMV were constructed. Infectivity of the AS mutants in the host plant Chenopodium quinoa showed that the central region of BMV MP is important for viral movement and both termini of BMV MP have effects on the development of systemic symptoms. A green-fluorescent-protein-expressing RNA3-based BMV vector containing a 2A sequence from Foot-and-mouth disease virus was also constructed. Using this vector, two AS mutants that showed more efficient cell-to-cell movement than wild-type BMV were identified. The MPs of these two AS mutants, which have mutations at their C termini, mediated cell-to-cell movement independently of coat protein (CP), unlike wild-type BMV MP. Furthermore, a BMV mutant with a truncation in the C-terminal 42 amino acids of MP was also able to move from cell to cell without CP, but did not move systemically, even in the presence of CP. These results and an encapsidation analysis suggest that the C terminus of BMV MP is involved in the requirement for CP in cell-to-cell movement and plays a role in long-distance movement. Furthermore, the ability to spread locally and form virions is not sufficient for the long-distance movement of BMV. The roles of MP and CP in BMV movement are discussed.

scholarly journals Viral cell-to-cell movement requires formation of cortical punctate structures containing Red clover necrotic mosaic virus movement protein

Virology ◽  
2011 ◽  
Vol 413 (2) ◽  
pp. 205-215 ◽  
Author(s):  
Masanori Kaido ◽  
Naoko Funatsu ◽  
Yasuko Tsuno ◽  
Kazuyuki Mise ◽  
Tetsuro Okuno
Keyword(s):  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Red Clover ◽  
Virus Movement

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

Virology ◽  
2005 ◽  
Vol 333 (1) ◽  
pp. 10-21 ◽  
Author(s):  
Douglas Tremblay ◽  
Andrew A. Vaewhongs ◽  
Katherine A. Turner ◽  
Tim L. Sit ◽  
Steven A. Lommel
Keyword(s):  
Cell Wall ◽  
Mosaic Virus ◽  
Movement Protein ◽  
Cell Movement ◽  
Red Clover ◽  
Virus Movement

scholarly journals Compatibility of the movement protein and the coat protein of cucumoviruses is required for cell-to-cell movement

2004 ◽  
Vol 85 (4) ◽  
pp. 1039-1048 ◽  
Author(s):  
Katalin Salánki ◽  
Ákos Gellért ◽  
Emese Huppert ◽  
Gábor Náray-Szabó ◽  
Ervin Balázs
Keyword(s):  
Coat Protein ◽  
Movement Protein ◽  
Point Mutations ◽  
Cell Movement ◽  
Virus Movement ◽  
Tomato Aspermy Virus ◽  
Sequence Encoding ◽  
Surface Electrostatic Potential ◽  
Test Plants ◽  
Insight Into

For the cell-to-cell movement of cucumoviruses both the movement protein (MP) and the coat protein (CP) are required. These are not reversibly exchangeable between Cucumber mosaic virus (CMV) and Tomato aspermy virus (TAV). The MP of CMV is able to function with the TAV CP (chimera RT), but TAV MP is unable to promote the cell-to-cell movement in the presence of CMV CP (chimera TR). To gain further insight into the non-infectious nature of the TR recombinant, RNA 3 chimeras were constructed with recombinant MPs and CPs. The chimeric MP and one of the CP recombinants were infectious. The other recombinant CP enabled virus movement only after the introduction of two point mutations (Glu→Lys and Lys→Arg at aa 62 and 65, respectively). The mutations served to correct the CP surface electrostatic potential that was altered by the recombination. The infectivity of the TR virus on different test plants was restored by replacing the sequence encoding the C-terminal 29 aa of the MP with the corresponding sequence of the CMV MP gene or by exchanging the sequence encoding the C-terminal 15 aa of the CP with the same region of TAV. The analysis of the recombinant clones suggests a requirement for compatibility between the C-terminal 29 aa of the MP and the C-terminal two-thirds of the CP for cell-to-cell movement of cucumoviruses.

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