scholarly journals Cell-to-cell movement of Alfalfa mosaic virus can be mediated by the movement proteins of Ilar-, bromo-, cucumo-, tobamo- and comoviruses and does not require virion formation

Virology ◽  
2006 ◽  
Vol 346 (1) ◽  
pp. 66-73 ◽  
Author(s):  
Jesús A. Sánchez-Navarro ◽  
María Carmen Herranz ◽  
Vicente Pallás
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Cell Movement ◽  
Movement Proteins ◽  
Virion Formation

scholarly journals Cell-to-Cell Movement of Beet Necrotic Yellow Vein Virus: I. Heterologous Complementation Experiments Provide Evidence for Specific Interactions Among the Triple Gene Block Proteins

1998 ◽  
Vol 11 (7) ◽  
pp. 618-625 ◽  
Author(s):  
Emmanuelle Lauber ◽  
Claudine Bleykasten-Grosshans ◽  
M. Erhardt ◽  
S. Bouzoubaa ◽  
G. Jonard ◽  
...  
Keyword(s):  
Mosaic Virus ◽  
Triple Gene Block ◽  
Chenopodium Quinoa ◽  
Alfalfa Mosaic Virus ◽  
Cell Movement ◽  
Yellow Vein ◽  
Specific Interactions ◽  
In Planta ◽  
Movement Proteins ◽  
Gene Block

Cell-to-cell movement of beet necrotic yellow vein virus (BNYVV) requires three proteins encoded by a triple gene block (TGB) on viral RNA 2. A BNYVV RNA 3-derived replicon was used to express movement proteins of other viruses and the ability of these proteins to functionally substitute for the BNYVV TGB proteins was tested by coinoculation of TGB-defective BNYVV with the various replicons to Chenopodium quinoa. Trans-heterocomplementation was successful with the movement protein (P30) of tobacco mosaic virus but not with the tubule-forming movement proteins of alfalfa mosaic virus and grapevine fanleaf virus. Trans-complementation of BNYVV movement was also observed when all three TGB proteins of the distantly related peanut clump virus were supplied together but not when they were substituted for their BNYVV counterparts one by one. When P30 was used to drive BNYVV movement in trans, accumulation of the first TGB protein of BNYVV was adversely affected by null mutations in the second and third TGB proteins. Taken together, these results suggest that highly specific interactions among cognate TGB proteins are important for their function and/or stability in planta.

scholarly journals Cucumber mosaic virus 2a polymerase and 3a movement proteins independently affect both virus movement and the timing of symptom development in zucchini squash

2005 ◽  
Vol 86 (4) ◽  
pp. 1213-1222 ◽  
Author(s):  
Seung Kook Choi ◽  
Peter Palukaitis ◽  
Byoung Eun Min ◽  
Mi Yeon Lee ◽  
Jang Kyung Choi ◽  
...  
Keyword(s):  
Cucumber Mosaic Virus ◽  
Mosaic Virus ◽  
Cell Movement ◽  
Virus Movement ◽  
Differential Rate ◽  
Systemic Symptom ◽  
Symptom Development ◽  
Movement Proteins ◽  
The Difference ◽  
Systemic Symptoms

The basis for differences in the timing of systemic symptom elicitation in zucchini squash between a pepper strain of Cucumber mosaic virus (Pf-CMV) and a cucurbit strain (Fny-CMV) was analysed. The difference in timing of appearance of systemic symptoms was shown to map to both RNA 2 and RNA 3 of Pf-CMV, with pseudorecombinant viruses containing either RNA 2 or RNA 3 from Pf-CMV showing an intermediate rate of systemic symptom development compared with those containing both or neither Pf-CMV RNAs. Symptom phenotype was shown to map to two single-nucleotide changes, both in codons for Ile at aa 267 and 168 (in Fny-CMV RNAs 2 and 3, respectively) to Thr (in Pf-CMV RNAs 2 and 3). The differential rate of symptom development was shown to be due to differences in the rates of cell-to-cell movement in the inoculated cotyledons, as well as differences in the rate of egress of the virus from the inoculated leaves. These data indicate that both the CMV 3a movement protein and the CMV 2a polymerase protein affect the rate of movement of CMV in zucchini squash and that these two proteins function independently of each other in their interactions with the host, facilitating virus movement.

scholarly journals Interaction of DNA with the Movement Proteins of Geminiviruses Revisited

2004 ◽  
Vol 78 (14) ◽  
pp. 7698-7706 ◽  
Author(s):  
Stefan Hehnle ◽  
Christina Wege ◽  
Holger Jeske
Keyword(s):  
Electron Microscopy ◽  
Mosaic Virus ◽  
Plasma Membranes ◽  
Transport Model ◽  
Cell Movement ◽  
Apparent Size ◽  
Cooperative Interaction ◽  
Mobility Shift ◽  
Movement Proteins ◽  
Gel Mobility Shift

ABSTRACT Geminiviruses manage the transport of their DNA within plants with the help of three proteins, the coat protein (CP), the nuclear shuttle protein (NSP), and the movement protein (MP). The DNA-binding capabilities of CP, NSP, and MP of Abutilon mosaic virus (AbMV; family Geminiviridae; genus Begomovirus) were scrutinized using gel mobility shift assays and electron microscopy. CP and NSP revealed a sequence-independent affinity for both double-stranded and single-stranded DNA, as has been previously reported for other begomoviruses. MP interacted selectively with dimeric supercoiled plasmid DNA in the electrophoretic assay. Further apparent size- and form-selective binding capacities of MP have been previously reported for another geminivirus (Bean dwarf mosaic virus), but in the case of AbMV, they have been identified as the result of electrophoretic interference rather than of complex formation. Without these complications, electron microscopy confirmed the assembly of double-stranded supercoiled DNA with NSP and MP into conspicuous structures and provided the first direct evidence for cooperative interaction of MP, NSP, and DNA. Based on these results and previous ones, a transport model of geminiviruses is discussed in which NSP packages DNA and MP anchors this complex to the protoplasmic leaflets of plasma membranes and microsomes for cell-to-cell movement.

scholarly journals Multifunctional Roles for the N-Terminal Basic Motif of Alfalfa mosaic virus Coat Protein: Nucleolar/Cytoplasmic Shuttling, Modulation of RNA-Binding Activity, and Virion Formation

2012 ◽  
Vol 25 (8) ◽  
pp. 1093-1103 ◽  
Author(s):  
Mari Carmen Herranz ◽  
Vicente Pallas ◽  
Frederic Aparicio
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Nuclear Export ◽  
Rna Binding ◽  
Nuclear Export Signal ◽  
Alfalfa Mosaic Virus ◽  
Binding Activity ◽  
Systemic Movement ◽  
Virion Formation

In addition to virion formation, the coat protein (CP) of Alfalfa mosaic virus (AMV) is involved in the regulation of replication and translation of viral RNAs, and in cell-to-cell and systemic movement of the virus. An intriguing feature of the AMV CP is its nuclear and nucleolar accumulation. Here, we identify an N-terminal lysine-rich nucleolar localization signal (NoLS) in the AMV CP required to both enter the nucleus and accumulate in the nucleolus of infected cells, and a C-terminal leucine-rich domain which might function as a nuclear export signal. Moreover, we demonstrate that AMV CP interacts with importin-α, a component of the classical nuclear import pathway. A mutant AMV RNA 3 unable to target the nucleolus exhibited reduced plus-strand RNA synthesis and cell-to-cell spread. Moreover, virion formation and systemic movement were completely abolished in plants infected with this mutant. In vitro analysis demonstrated that specific lysine residues within the NoLS are also involved in modulating CP-RNA binding and CP dimerization, suggesting that the NoLS represents a multifunctional domain within the AMV CP. The observation that nuclear and nucleolar import signals mask RNA-binding properties of AMV CP, essential for viral replication and translation, supports a model in which viral expression is carefully modulated by a cytoplasmic/nuclear balance of CP accumulation.

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.

The Roles of the Red Clover Necrotic Mosaic Virus Capsid and Cell-to-Cell Movement Proteins in Systemic Infection

Virology ◽  
1993 ◽  
Vol 192 (1) ◽  
pp. 27-32 ◽  
Author(s):  
Z. Xiong ◽  
K.H. Kim ◽  
D. Giesman-Cookmeyer ◽  
S.A. Lommel
Keyword(s):  
Mosaic Virus ◽  
Cell Movement ◽  
Systemic Infection ◽  
Red Clover ◽  
Virus Capsid ◽  
Movement Proteins

scholarly journals Receptor-like kinase BAM1 facilitates early movement of the Tobacco mosaic virus

2021 ◽  
Vol 4 (1) ◽  
Author(s):  
Phu-Tri Tran ◽  
Vitaly Citovsky
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Cell Movement ◽  
Protein Kinase Activity ◽  
Loss Of Function ◽  
Negative Effects ◽  
Movement Proteins ◽  
Cellular Factors ◽  
Receptor Like Kinase

AbstractCell-to-cell movement is an important step for initiation and spreading of virus infection in plants. This process occurs through the intercellular connections, termed plasmodesmata (PD), and is usually mediated by one or more virus-encoded movement proteins (MP) which interact with multiple cellular factors, among them protein kinases that usually have negative effects on MP function and virus movement. In this study, we report physical and functional interaction between MP of Tobacco mosaic virus (TMV), the paradigm of PD-moving proteins, and a receptor-like kinase BAM1 from Arabidopsis and its homolog from Nicotiana benthamiana. The interacting proteins accumulated in the PD regions, colocalizing with a PD marker. Reversed genetics experiments, using BAM1 gain-of-function and loss-of-function plants, indicated that BAM1 is required for efficient spread and accumulation the virus during initial stages of infection of both plant species by TMV. Furthermore, BAM1 was also required for the efficient cell-to-cell movement of TMV MP, suggesting that BAM1 interacts with TMV MP to support early movement of the virus. Interestingly, this role of BAM1 in viral movement did not require its protein kinase activity. Thus, we propose that association of BAM1 with TMV MP at PD facilitates the MP transport through PD, which, in turn, enhances the spread of the viral infection.

scholarly journals Tm-22 Resistance in Tomato Requires Recognition of the Carboxy Terminus of the Movement Protein of Tomato Mosaic Virus

1998 ◽  
Vol 11 (6) ◽  
pp. 498-503 ◽  
Author(s):  
Hans Weber ◽  
Artur J. P. Pfitzner
Keyword(s):  
Mosaic Virus ◽  
Resistance Gene ◽  
Movement Protein ◽  
Cell Movement ◽  
Tomato Mosaic Virus ◽  
Wild Type ◽  
Virus Transport ◽  
Tomato Plants ◽  
Movement Proteins ◽  
Carboxy Terminal

The Tm-22 resistance gene is used in most commercial tomato cultivars for protection against infection with tomato mosaic virus (ToMV). It has been suggested that Tm-22 resistance interferes with viral cell-to-cell movement in plants; ToMV strain ToMV-22 requires two amino acid (aa) exchanges in the carboxy-terminal region of the viral 30-kDa movement protein (at positions 238 and 244) to overcome Tm-22 resistance. For further analysis of this region of the 30-kDa protein, two stop codons were introduced into ToMV movement proteins at aa positions 235 and 237, leading to deletion of the terminal 30 aa. The mutant virus strains were able to infect wild-type tomato plants systemically, suggesting the carboxy-terminal portion of the ToMV 30-kDa protein is dispensable for virus transport in tomato. Even more important, the deletion mutants overcame the Tm-22 resistance gene. These data indicate the carboxy-terminal domain of the ToMV movement protein serves as a recognition target in the context of the Tm-22 resistance gene. Furthermore, expression of the 30-kDa movement protein from wild-type ToMV, but not from ToMV-22, in transgenic tomato plants with the Tm-22 resistance gene led to elicitation of a necrotic reaction in tomato seedlings, showing that the 30-kDa protein on its own is able to induce the plant's defense reaction.

scholarly journals The N-terminal Region of the Plantago asiatica mosaic virus Coat Protein Is Required for Cell-to-Cell Movement but Is Dispensable for Virion Assembly

2009 ◽  
Vol 22 (6) ◽  
pp. 677-685 ◽  
Author(s):  
Johji Ozeki ◽  
Masayoshi Hashimoto ◽  
Ken Komatsu ◽  
Kensaku Maejima ◽  
Misako Himeno ◽  
...  
Keyword(s):  
Coat Protein ◽  
Mosaic Virus ◽  
Cell Movement ◽  
Terminal Region ◽  
Reading Frame ◽  
Movement Proteins ◽  
Virus Accumulation ◽  
Viral Spread ◽  
Plantago Asiatica

Potexvirus cell-to-cell movement requires coat protein (CP) and movement proteins. In this study, mutations in two conserved in-frame AUG codons in the 5′ region of the CP open reading frame of Plantago asiatica mosaic virus (PlAMV) were introduced, and virus accumulation of these mutants was analyzed in inoculated and upper noninoculated leaves. When CP was translated only from the second AUG codon, virus accumulation in inoculated leaves was lower than that of wild-type PlAMV, and the viral spread was impaired. Trans-complementation analysis showed that the leucine residue at the third position (Leu-3) of CP is important for cell-to-cell movement of PlAMV. The 14-amino-acid N-terminal region of CP was dispensable for virion formation. Immunoprecipitation assays conducted with an anti-TGBp1 antibody indicated that PlAMV CP interacts with TGBp1 in vivo and that this interaction is not affected by alanine substitution at Leu-3. These results support the concept that the N-terminal region of potexvirus CP can be separated into two distinct functional domains.

scholarly journals Tubule-forming capacity of the movement proteins of alfalfa mosaic virus and brome mosaic virus.

1997 ◽  
Vol 78 (8) ◽  
pp. 2089-2093 ◽  
Author(s):  
D T Kasteel ◽  
R W Goldbach ◽  
K A Jansen ◽  
J W van Lent ◽  
N N van der Wel
Keyword(s):  
Mosaic Virus ◽  
Alfalfa Mosaic Virus ◽  
Brome Mosaic Virus ◽  
Movement Proteins
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