Interaction of <i>Sesbania</i> mosaic virus movement protein with the coat protein – implications for viral spread

Chowdhury, Soumya Roy; Savithri, H.S.

doi:10.1111/j.1742-4658.2010.07943.x

Cited by 23 publications

(17 citation statements)

References 49 publications

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“…The analysis of the spectrum using K2D2 software suggested that NSm is predominantly (81%) an alpha helical protein. Recently, it was shown that Sesbania Mosaic Virus (SeMV) MP is also a helical protein which interacts with its CP [37]. Other helical proteins well characterized for their role in movement are Tobacco mosaic virus (TMV) MP [38], TGBp1 of hordeivirus [39] and P7 of carmovirus [8].…”

Section: Resultsmentioning

confidence: 99%

Groundnut Bud Necrosis Virus Encoded NSm Associates with Membranes via Its C-Terminal Domain

2014

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Groundnut Bud Necrosis Virus (GBNV) is a tripartite ambisense RNA plant virus that belongs to serogroup IV of Tospovirus genus. Non-Structural protein-m (NSm), which functions as movement protein in tospoviruses, is encoded by the M RNA. In this communication, we demonstrate that despite the absence of any putative transmembrane domain, GBNV NSm associates with membranes when expressed in E. coli as well as in N. benthamiana. Incubation of refolded NSm with liposomes ranging in size from 200–250 nm resulted in changes in the secondary and tertiary structure of NSm. A similar behaviour was observed in the presence of anionic and zwitterionic detergents. Furthermore, the morphology of the liposomes was found to be modified in the presence of NSm. Deletion of coiled coil domain resulted in the inability of in planta expressed NSm to interact with membranes. Further, when the C-terminal coiled coil domain alone was expressed, it was found to be associated with membrane. These results demonstrate that NSm associates with membranes via the C-terminal coiled coil domain and such an association may be important for movement of viral RNA from cell to cell.

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Section: Resultsmentioning

confidence: 99%

Groundnut Bud Necrosis Virus Encoded NSm Associates with Membranes via Its C-Terminal Domain

2014

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“…Another example of CP-MP interaction was reported for Sesbania mosaic sobemovirus (SeMV) (Chowdhury and Savithri, 2011). The Escherichia coli-expressed SeMV MP interacted with the native viral particles through the N-terminal 49 amino acid MP domain.…”

Section: Cps and Virus Movementmentioning

confidence: 97%

Multiple functions of capsid proteins in (+) stranded RNA viruses during plant–virus interactions

Weber

Bujarski

2015

Virus Research

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“…Moreover, long distance movement of RYMV and SCPMV has been proposed to be dependent on viral particle formation [16,17]. The CP of Sesbania mosaic virus (SeMV) has been shown to interact with P1, which is a suppressor of RNA silencing and has been implicated in virus movement [18-20]. …”

Section: Introductionmentioning

confidence: 99%

Cocksfoot mottle virus coat protein is dispensable for the systemic infection

Olspert

Kamsol

Sarmiento

et al. 2014

Virol J

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BackgroundThe Sobemovirus genome consists of polycistronic single-stranded positive-sense RNA. The first ORF encodes P1, a suppressor of RNA silencing required for virus movement. The coat protein (CP) is expressed from the 3′ proximal ORF3 via subgenomic RNA. In addition to its structural role, the CP of some sobemoviruses has been reported to be required for systemic movement and to interact with P1. The aim of this study was to analyse the role of Cocksfoot mottle virus (CfMV) CP in the suppression of RNA silencing and virus movement.MethodsAgrobacterium-mediated transient expression method was used for testing CfMV CP capacity to suppress RNA silencing. CP substitution and deletion mutants were generated to examine the role of this protein in CfMV infection, using three host plants (oat, barley and wheat). The viral movement was characterised with CfMV expressing EGFP fused to the C-terminus of CP.ResultsIn the current study we show that CfMV CP is an additional RNA silencing suppressor. Interestingly, we observed that all CP mutant viruses were able to infect the three tested host plants systemically, although usually with reduced accumulation. CfMV expressing EGFP was detected in epidermal and mesophyll cells of inoculated leaves. Although EGFP fluorescence was not detected in upper leaves, some plants displayed CfMV symptoms. Analysis of the upper leaves revealed that the viruses had lost the EGFP sequence and sometimes also most of the CP gene.ConclusionsThe present study demonstrates that CfMV CP suppresses RNA silencing but, surprisingly, is dispensable for systemic movement. Thus, CfMV does not move as virion in the tested host plants. The composition of the movement RNP complex remains to be elucidated.

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Interaction of Sesbania mosaic virus movement protein with the coat protein – implications for viral spread

Cited by 23 publications

References 49 publications

Groundnut Bud Necrosis Virus Encoded NSm Associates with Membranes via Its C-Terminal Domain

Groundnut Bud Necrosis Virus Encoded NSm Associates with Membranes via Its C-Terminal Domain

Multiple functions of capsid proteins in (+) stranded RNA viruses during plant–virus interactions

Cocksfoot mottle virus coat protein is dispensable for the systemic infection

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