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.

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 Citrus Psorosis Virus Movement Protein Contains an Aspartic Protease Required for Autocleavage and the Formation of Tubule-Like Structures at Plasmodesmata

2018 ◽  
Vol 92 (21) ◽  
Author(s):  
Gabriel Robles Luna ◽  
Eduardo José Peña ◽  
María Belén Borniego ◽  
Manfred Heinlein ◽  
María Laura García
Keyword(s):  
Protease Activity ◽  
Movement Protein ◽  
Cell Movement ◽  
Cleavage Product ◽  
Aspartic Protease ◽  
Virus Movement ◽  
Tubule Formation ◽  
Content Type ◽  
Amino Terminal ◽  
Citrus Psorosis Virus

ABSTRACTPlant virus cell-to-cell movement is an essential step in viral infections. This process is facilitated by specific virus-encoded movement proteins (MPs), which manipulate the cell wall channels between neighboring cells known as plasmodesmata (PD). Citrus psorosis virus (CPsV) infection in sweet orange involves the formation of tubule-like structures within PD, suggesting that CPsV belongs to “tubule-forming” viruses that encode MPs able to assemble a hollow tubule extending between cells to allow virus movement. Consistent with this hypothesis, we show that the MP of CPsV (MPCPsV) indeed forms tubule-like structures at PD upon transient expression inNicotiana benthamianaleaves. Tubule formation by MPCPsVdepends on its cleavage capacity, mediated by a specific aspartic protease motif present in its primary sequence. A single amino acid mutation in this motif abolishes MPCPsVcleavage, alters the subcellular localization of the protein, and negatively affects its activity in facilitating virus movement. The amino-terminal 34-kDa cleavage product (34KCPsV), but not the 20-kDa fragment (20KCPsV), supports virus movement. Moreover, similar to tubule-forming MPs of other viruses, MPCPsV(and also the 34KCPsVcleavage product) can homooligomerize, interact with PD-located protein 1 (PDLP1), and assemble tubule-like structures at PD by a mechanism dependent on the secretory pathway. 20KCPsVretains the protease activity and is able to cleave a cleavage-deficient MPCPsVintrans. Altogether, these results demonstrate that CPsV movement depends on the autolytic cleavage of MPCPsVby an aspartic protease activity, which removes the 20KCPsVprotease and thereby releases the 34KCPsVprotein for PDLP1-dependent tubule formation at PD.IMPORTANCEInfection by citrus psorosis virus (CPsV) involves a self-cleaving aspartic protease activity within the viral movement protein (MP), which results in the production of two peptides, termed 34KCPsVand 20KCPsV, that carry the MP and viral protease activities, respectively. The underlying protease motif within the MP is also found in the MPs of other members of theAspiviridaefamily, suggesting that protease-mediated protein processing represents a conserved mechanism of protein expression in this virus family. The results also demonstrate that CPsV and potentially other ophioviruses move by a tubule-guided mechanism. Although several viruses from different genera were shown to use this mechanism for cell-to-cell movement, our results also demonstrate that this mechanism is controlled by posttranslational protein cleavage. Moreover, given that tubule formation and virus movement could be inhibited by a mutation in the protease motif, targeting the protease activity for inactivation could represent an important approach for ophiovirus control.

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

2003 ◽  
Vol 84 (3) ◽  
pp. 727-732 ◽  
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.

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.

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