scholarly journals Spontaneous Mutation in the Movement Protein of Citrus Leprosis Virus C2, in a Heterologous Virus Infection Context, Increases Cell-to-Cell Transport and Generates Fitness Advantage

Viruses ◽  
2021 ◽  
Vol 13 (12) ◽  
pp. 2498
Author(s):  
Mikhail Oliveira Leastro ◽  
David Villar-Álvarez ◽  
Juliana Freitas-Astúa ◽  
Elliot Watanabe Kitajima ◽  
Vicente Pallás ◽  
...  
Keyword(s):  
Movement Protein ◽  
Spontaneous Mutation ◽  
Alfalfa Mosaic Virus ◽  
Viral Fitness ◽  
Viral Population ◽  
Long Distance ◽  
Cell Transport ◽  
Fitness Advantage ◽  
Citrus Leprosis ◽  
Virus C

Previous results using a movement defective alfalfa mosaic virus (AMV) vector revealed that citrus leprosis virus C (CiLV-C) movement protein (MP) generates a more efficient local movement, but not more systemic transport, than citrus leprosis virus C2 (CiLV-C2) MP, MPs belonging to two important viruses for the citrus industry. Here, competition experiment assays in transgenic tobacco plants (P12) between transcripts of AMV constructs expressing the cilevirus MPs, followed by several biological passages, showed the prevalence of the AMV construct carrying the CiLV-C2 MP. The analysis of AMV RNA 3 progeny recovered from P12 plant at the second viral passage revealed the presence of a mix of progeny encompassing the CiLV-C2 MP wild type (MPWT) and two variants carrying serines instead phenylalanines at positions 72 (MPS72F) or 259 (MPS259F), respectively. We evaluated the effects of each modified residue in virus replication, and cell-to-cell and long-distance movements. Results indicated that phenylalanine at position 259 favors viral cell-to-cell transport with an improvement in viral fitness, but has no effect on viral replication, whereas mutation at position 72 (MPS72F) has a penalty in the viral fitness. Our findings indicate that the prevalence of a viral population may be correlated with its greater efficiency in cell-to-cell and systemic movements.

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.

scholarly journals In vitro expression and antiserum production against the movement protein of Citrus leprosis virus C (CiLV-C)

2012 ◽  
Vol 37 (2) ◽  
pp. 136-141 ◽  
Author(s):  
Renata F. Calegario ◽  
Mônica T.V. Labate ◽  
Luís A. Peroni ◽  
Dagmar Ruth Stach-Machado ◽  
Maxuel O. Andrade ◽  
...  
Keyword(s):  
Movement Protein ◽  
In Vitro Expression ◽  
Citrus Leprosis ◽  
Virus C

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.

Alfalfa mosaic virus temperature-sensitive mutants III. Mutants with a putative defect in cell-to-cell transport

Virology ◽  
1986 ◽  
Vol 154 (2) ◽  
pp. 401-404 ◽  
Author(s):  
Marianne J. Huisman ◽  
Alberto N. Sarachu ◽  
Fieke Ablas ◽  
Helgo J.G. Broxterman ◽  
Lous Van Vloten-Doting ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Temperature Sensitive ◽  
Cell Transport ◽  
Temperature Sensitive Mutants

scholarly journals Potyviral 6K2 Protein Long-Distance Movement and Symptom-Induction Functions Are Independent and Host-Specific

2004 ◽  
Vol 17 (5) ◽  
pp. 502-510 ◽  
Author(s):  
Carl Spetz ◽  
Jari P. T. Valkonen
Keyword(s):  
Spontaneous Mutation ◽  
Systemic Infection ◽  
Wild Type ◽  
Virus Propagation ◽  
Long Distance ◽  
Potato Virus A ◽  
Viral Mutant ◽  
Membrane Bound ◽  
Long Distance Movement

Deletion of various portions, or insertion of six histidine residues (6×His) into various positions of the membrane-bound 6K2 protein (53 amino acids) of Potato virus A (PVA, genus Potyvirus), inhibited systemic infection in Nicotiana tabacum and N. benthamiana plants. However, a spontaneous mutation (Gly2Cys) that occurred in 6K2 adjacent to the 6×His insert placed between Ser1 and Gly2 enabled systemic infection in a single N. benthamiana plant. No symptoms were observed, but virus titers were similar to the symptom-inducing wild-type (wt) PVA. N. tabacum plants were not systemically infected, albeit virus propagation was observed in inoculated protoplasts. The 6×His/Gly2Cys mutant was reconstructed in vitro and serially propagated by mechanical inoculation in N. benthamiana. Following the third passage, a novel viral mutant appeared, lacking the last four His residues of the insert, as well as the Gly2 and Thr3 of 6K2. It infected N. tabacum plants systemically, and in the systemically infected N. benthamiana leaves, vein chlorosis and mild yellowing symptoms were observed, typical of wt PVA infection. The mutant virus accumulated to titers similar to wt PVA in both hosts. These results show that the PVA 6K2 protein affects viral long-distance movement and symptom induction independently and in a host-specific manner.

scholarly journals Citrus Leprosis Virus C Encodes Three Proteins With Gene Silencing Suppression Activity

2020 ◽  
Vol 11 ◽  
Author(s):  
Mikhail Oliveira Leastro ◽  
Deibis Yorlenis Ortega Castro ◽  
Juliana Freitas-Astúa ◽  
Elliot Watanabe Kitajima ◽  
Vicente Pallás ◽  
...  
Keyword(s):  
Gene Silencing ◽  
Citrus Leprosis ◽  
Silencing Suppression ◽  
Virus C

scholarly journals Heterologous Movement Protein Strongly Modifies the Infection Phenotype of Cucumber Mosaic Virus

2002 ◽  
Vol 76 (7) ◽  
pp. 3554-3557 ◽  
Author(s):  
Emese Huppert ◽  
Dénes Szilassy ◽  
Katalin Salánki ◽  
Zoltán Divéki ◽  
Ervin Balázs
Keyword(s):  
Nicotiana Tabacum ◽  
Virus Infection ◽  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Host Plants ◽  
Movement Protein ◽  
Long Distance ◽  
Cucumber Mosaic Cucumovirus ◽  
Nicotiana Debneyi ◽  
Symptom Phenotype

ABSTRACT A hybrid virus (CMVcymMP) constructed by replacing the movement protein (MP) of cucumber mosaic cucumovirus (CMV) with that of cymbidium ringspot tombusvirus (CymRSV) was viable and could efficiently spread both cell to cell and long distance in host plants. The hybrid virus was able to move cell to cell in the absence of functional CP, whereas CP-deficient CMV was restricted to single inoculated cells. In several Chenopodium and Nicotiana species, the symptom phenotype of the hybrid virus infection was clearly determined by the foreign MP gene. In Nicotiana debneyi and Nicotiana tabacum cv. Xanthi, the hybrid virus could move systemically, contrary to CymRSV.

scholarly journals First Report of Brevipalpus papayensis as Vector of Coffee ringspot virus and Citrus leprosis virus C

Plant Disease ◽  
2018 ◽  
Vol 102 (5) ◽  
pp. 1046-1046 ◽  
Author(s):  
M. A. Nunes ◽  
J. L. de Carvalho Mineiro ◽  
L. A. Rogerio ◽  
L. M. Ferreira ◽  
A. Tassi ◽  
...  
Keyword(s):  
Ringspot Virus ◽  
First Report ◽  
Citrus Leprosis ◽  
Virus C

scholarly journals Membrane Association and Topology of Citrus Leprosis Virus C2 Movement and Capsid Proteins

2021 ◽  
Vol 9 (2) ◽  
pp. 418
Author(s):  
Mikhail Oliveira Leastro ◽  
Juliana Freitas-Astúa ◽  
Elliot Watanabe Kitajima ◽  
Vicente Pallás ◽  
Jesús Á. Sánchez-Navarro
Keyword(s):  
Capsid Protein ◽  
Movement Protein ◽  
Capsid Proteins ◽  
Membrane Association ◽  
Membrane Fractionation ◽  
Chemical Treatments ◽  
And Topology ◽  
Intracellular Movement ◽  
Citrus Leprosis ◽  
Biomolecular Fluorescence Complementation

Although citrus leprosis disease has been known for more than a hundred years, one of its causal agents, citrus leprosis virus C2 (CiLV-C2), is poorly characterized. This study described the association of CiLV-C2 movement protein (MP) and capsid protein (p29) with biological membranes. Our findings obtained by computer predictions, chemical treatments after membrane fractionation, and biomolecular fluorescence complementation assays revealed that p29 is peripherally associated, while the MP is integrally bound to the cell membranes. Topological analyses revealed that both the p29 and MP expose their N- and C-termini to the cell cytoplasmic compartment. The implications of these results in the intracellular movement of the virus were discussed.

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