The C-terminal 33 amino acids of the cucumber mosaic virus 3a protein affect virus movement, RNA binding and inhibition of infection and translation

Kim, Sang Hyon; Калинина, Н. В.; Андреев, И. А.; Ryabov, Eugene V.; Fitzgerald, A. G.; Taliansky, Michael; Palukaitis, Peter

doi:10.1099/vir.0.19583-0

Cited by 51 publications

(33 citation statements)

References 34 publications

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“…This suggestion is supported by our covariation analyses, which reveal that the C-terminal amino acids of MP are coevolving with the N-terminal region of CP (CP CG1). This suggestion gets further support from evidence for such contact in other members of the Bromoviridae family such as CMV (26), BMV (47), and AMV (41,43).…”

Section: Discussionmentioning

confidence: 74%

“…Furthermore, recently Sánchez-Navarro et al (43) have shown that the 44 amino acids at the AMV MP C terminus physically interact with CP to elicit movement. Apparently, the C terminus of AMV MP confers specificity on the transport process (41) as it does in the cases of BMV (47) and CMV (26). MPs of PNRSV, AMV, CMV, and BMV have been shown to have an RNA-binding domain located at the N terminus of the protein in the first two cases or at the C terminus in the last two (3,4,7,21).…”

mentioning

confidence: 99%

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Adaptive Covariation between the Coat and Movement Proteins of Prunus Necrotic Ringspot Virus

Codoñer

Fares

Elena

2006

J Virol

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The relative functional and/or structural importance of different amino acid sites in a protein can be assessed by evaluating the selective constraints to which they have been subjected during the course of evolution. Here we explore such constraints at the linear and three-dimensional levels for the movement protein (MP) and coat protein (CP) encoded by RNA 3 of prunus necrotic ringspot ilarvirus (PNRSV). By a maximum-parsimony approach, the nucleotide sequences from 46 isolates of PNRSV varying in symptomatology, host tree, and geographic origin have been analyzed and sites under different selective pressures have been identified in both proteins. We have also performed covariation analyses to explore whether changes in certain amino acid sites condition subsequent variation in other sites of the same protein or the other protein. These covariation analyses shed light on which particular amino acids should be involved in the physical and functional interaction between MP and CP. Finally, we discuss these findings in the light of what is already known about the implication of certain sites and domains in structure and protein-protein and RNA-protein interactions.

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Section: Discussionmentioning

confidence: 74%

mentioning

confidence: 99%

Adaptive Covariation between the Coat and Movement Proteins of Prunus Necrotic Ringspot Virus

Codoñer

Fares

Elena

2006

J Virol

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“…The failure to accumulate in upper leaves is probably due to an inability of D RNA 3-1 to move systemically in the absence of encapsidation rather than an inhibition of cellto-cell movement, since the latter process does not require either encapsidation or interaction between CMV RNAs and the capsid protein (Kim et al, 2004). It seems likely that virion formation is essential for systemic movement in squash, since it was shown that CMV capsid protein mutants that did not form virions still supported systemic movement in some Nicotiana species but not in squash .…”

Section: Discussionmentioning

confidence: 99%

Host-specific encapsidation of a defective RNA 3 of Cucumber mosaic virus

Kaplan

Lee

Canto³

et al. 2004

Journal of General Virology

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Defective (D) RNAs were generated in tobacco upon passage of two isolates of Cucumber mosaic virus (CMV) initially derived from RNA transcripts of cDNA clones. In both cases, the D RNA was derived by a single in-frame deletion of either 339 or 411 nt within the 3a gene of Fny-CMV RNA 3 or M-CMV RNA 3, respectively. The generation of D RNAs was rare and occurred with two CMV isolates, the virions of which were known to differ in physico-chemical properties.The Fny-CMV D RNA 3, designated D RNA 3-1, was maintained by passage together with Fny-CMV in tobacco, but was lost by passage in squash. D RNA 3-1 accumulated in the inoculated squash cotyledons but not in upper, systemically infected leaves. Virions purified from infected squash cotyledons or leaf mesophyll protoplasts did not contain D RNA 3-1. Therefore, the failure of D RNA 3-1 to accumulate in squash leaves systemically infected by CMV was due to a lack of encapsidation of the D RNA 3-1 and movement out of the inoculated leaves.

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“…replication and/or translation; Bol, 2005). In the case of the CMV MP, the deletion of the dispensable C terminus region induced an increase of the MP RNA-binding affinity, indicating that perhaps both effects, the lack of the C terminus and the increasing of the RNA affinity, could be required to convert a CP-dependent protein into a CP-independent one (Kim et al, 2004). In BMV, MP-CP interaction requires mature virion formation although an isolate has been described, capable to infect dicot plants, that is able to move between cells independently of CP (Takeda et al, 2004(Takeda et al, , 2005.…”

Section: Analysis Of the C-terminal Region Of Pnrsv Mpmentioning

confidence: 99%

Implication of the C terminus of the Prunus necrotic ringspot virus movement protein in cell-to-cell transport and in its interaction with the coat protein

Aparicio

Pallás

Sánchez‐Navarro

2010

Journal of General Virology

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The movement protein (MP) of Prunus necrotic ringspot virus (PNRSV) is required for viral transport. Previous analysis with MPs of other members of the family Bromoviridae has shown that the C-terminal part of these MPs plays a critical role in the interaction with the cognate coat protein (CP) and in cell-to-cell transport. Bimolecular fluorescence complementation and overlay analysis confirm an interaction between the C-terminal 38 aa of PNRSV MP and its cognate CP. Mutational analysis of the C-terminal region of the PNRSV MP revealed that its C-terminal 38 aa are dispensable for virus transport, however, the 4 aa preceding the dispensable C terminus are necessary to target the MP to the plasmodesmata and for the functionality of the protein. The capacity of the PNRSV MP to use either a CP-dependent or a CP-independent cell-to-cell transport is discussed.Prunus necrotic ringspot virus (PNRSV) belongs to the genus Ilarvirus (family Bromoviridae). The PNRSV genome consists of three, single-stranded, plus-sense RNAs. RNAs 1 and 2 encode P1 and P2 polymerase protein subunits, respectively. RNA 3 directly encodes the movement protein (MP), whereas the coat protein (CP) is synthesized via a subgenomic RNA 4 (Sánchez-Navarro & Pallás, 1997).The MP of PNRSV belongs to the 30K superfamily (Melcher, 2000). The C-terminal region of the 30K MPs has a predicted random coiled secondary structure (Melcher, 2000). The alfalfa mosaic virus (AMV) MP specifically interacts with its cognate CP through its Cterminal region and in the cowpea mosaic virus (CPMV) MP this region is the virion-binding domain (Carvalho et al., 2003; Sánchez-Navarro et al., 2006). In the case of the MP of the cauliflower mosaic virus (CaMV), the C terminus interacts indirectly with the cognate CP via the virion-associated protein (Stavolone et al., 2005). The Cterminal region of the corresponding MPs of the cucumber mosaic virus (CMV) and the brome mosaic virus (BMV) controls the requirement of the CP for intercellular movement (Nagano et al., 2001; Sánchez-Navarro & Bol, 2001;Takeda et al., 2004). Deletion of the C-terminal 55 aa of the tobacco mosaic virus (TMV) MP does not affect the cell-to-cell transport of the TMV nor the cell-wall localization of the protein (Berna et al., 1991). In the present study, we have analysed the role of cell-to-cell movement of the PNRSV MP C-terminal region by mutational analysis. We also analysed the putative MP-CP interaction by bimolecular fluorescence complementation (BiFC) and overlay assays, respectively. Finally, we present data indicating that the capacity of the PNRSV MP to mediate virus transport is independent of the MP-CP interaction.Due to the lack of PNRSV infectious clones, a chimera cDNA3 construct between AMV and PNRSV that expresses the green fluorescent protein (GFP), the wild-type (wt) PNRSV MP fused in-frame to the C-terminal 44 aa of AMV MP (A44) and the AMV CP was used (clone pGFP/ MP-A44/CP in Sánchez-Navarro et al., 2006; hereafter pMP P -A44). The A44 is required for a specific interaction wit...

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The C-terminal 33 amino acids of the cucumber mosaic virus 3a protein affect virus movement, RNA binding and inhibition of infection and translation

Cited by 51 publications

References 34 publications

Adaptive Covariation between the Coat and Movement Proteins of Prunus Necrotic Ringspot Virus

Adaptive Covariation between the Coat and Movement Proteins of Prunus Necrotic Ringspot Virus

Host-specific encapsidation of a defective RNA 3 of Cucumber mosaic virus

Implication of the C terminus of the Prunus necrotic ringspot virus movement protein in cell-to-cell transport and in its interaction with the coat protein

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