Proteomic analysis of the plasma membrane-movement tubule complex of cowpea mosaic virus

Hollander, P. W. den; Duarte, Priscilla de Sousa Geraldino; Bloksma, H.R.; Boeren, Sjef; Lent, J.W.M. van

doi:10.1007/s00705-016-2757-3

Cited by 5 publications

(5 citation statements)

References 42 publications

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“…We cannot completely rule out an effect of competition between putative N. benthamiana , PDLP-like proteins and the transiently expressed A. thaliana PDLP1. However, in a recent proteomic analysis of the plasma membrane-tubule complex of CPMV in N. benthamiana no PDLP-like proteins were identified to be part of this complex isolated from infected protoplasts [ 27 ]. This and our present results suggest that PDLPs do not serve as a recognition/retention signal for MP accumulation.…”

Section: Discussionmentioning

confidence: 99%

The role of plasmodesma-located proteins in tubule-guided virus transport is limited to the plasmodesmata

Hollander

Kieper

Borst³

et al. 2016

Arch Virol

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Intercellular spread of plant viruses involves passage of the viral genome or virion through a plasmodesma (PD). Some viruses severely modify the PD structure, as they assemble a virion carrying tubule composed of the viral movement protein (MP) inside the PD channel. Successful modulation of the host plant to allow infection requires an intimate interaction between viral proteins and both structural and regulatory host proteins. To date, however, very few host proteins are known to promote virus spread. Plasmodesmata-located proteins (PDLPs) localised in the PD have been shown to contribute to tubule formation in cauliflower mosaic virus and grapevine fanleaf virus infections. In this study, we have investigated the role of PDLPs in intercellular transport of another tubule-forming virus, cowpea mosaic virus. The MP of this virus was found to interact with PDLPs in the PD, as was shown for other tubule-forming viruses. Expression of PDLPs and MPs in protoplasts in the absence of a PD revealed that these proteins do not co-localise at the site of tubule initiation. Furthermore, we show that tubule assembly in protoplasts does not require an interaction with PDLPs at the base of the tubule, as has been observed in planta. These results suggest that a physical interaction between MPs and PDLPs is not required for assembly of the movement tubule and that the beneficial role of PDLPs in virus movement is confined to the structural context of the PD.

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Section: Discussionmentioning

confidence: 99%

The role of plasmodesma-located proteins in tubule-guided virus transport is limited to the plasmodesmata

Hollander

Kieper

Borst³

et al. 2016

Arch Virol

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“…This process is known as intercellular or cell-to-cell movement [2], and to achieve it, plant viruses have developed various movement mechanisms [3]. Cowpea mosaic virus utilizes the whole viral particle to move through the PD [4], while Tobacco mosaic virus (TMV) moves as a viral ribonucleoprotein (vRNP) comprising the viral RNA, movement protein (MP), replicase, and host factors [5]. The virusencoded MPs play crucial roles in binding viral RNAs, expanding the PD, and allowing the virus to move to neighbouring cells [5][6][7][8].…”

Section: Introductionmentioning

confidence: 99%

The phosphorylation of the movement protein TGBp1 regulates the accumulation of the Bamboo mosaic virus

Wu,

Chen,

Hou

et al. 2024

Journal of General Virology

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Phosphorylation and dephosphorylation of viral movement proteins plays a crucial role in regulating virus movement. Our study focused on investigating the movement protein TGBp1 of Bamboo mosaic virus (BaMV), which is a single-stranded positive-sense RNA virus. Specifically, we examined four potential phosphorylation sites (S15, S18, T58, and S247) within the TGBp1 protein. To study the impact of phosphorylation, we introduced amino acid substitutions at the selected sites. Alanine substitutions were used to prevent phosphorylation, while aspartate substitutions were employed to mimic phosphorylation. Our findings suggest that mimicking phosphorylation at S15, S18 and T58 of TGBp1 might be linked to silencing suppressor activities. The phosphorylated form at these sites exhibits a loss of silencing suppressor activity, leading to reduced viral accumulation in the inoculated leaves. Furthermore, mimicking phosphorylation at residues S15 and S18 could diminish viral accumulation at the single-cell level, while doing so at residue T58 could influence virus movement. However, mimicking phosphorylation at residue S247 does not appear to be relevant to both functions of TGBp1. Overall, our study provides insights into the functional significance of specific phosphorylation sites in BaMV TGBp1, illuminating the regulatory mechanisms involved in virus movement and silencing suppression.

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“…Interestingly, the MPs of Brome mosaic virus (BMV; Genus Bromovirus ), Cucumber mosaic virus (CMV; Genus Cucumovirus ) and Red clover necrotic mosaic virus (RCNMV; genus Dianthovirus ) also interact with or colocalize with cognate replicases or VRCs and recruit VRCs to PD 34‐38 . Proteomic analysis of the plasma membrane‐tubular movement complexes of Cowpea mosaic virus (CPMV; Genus Comovirus ) revealed that viral MPs, small and large CPs and RdRps colocalize with host‐encoded PD‐localized proteins as well as host ribosomes and tRNAs 39 . The cytoplasmic ends of tubules associated with Broad bean wilt virus 2 (BBWV2; Genus Fabavirus ) VP37 are always associated with membrane structures similar to those involved in virus replication 40 .…”

Section: Introductionmentioning

confidence: 99%

“…[34][35][36][37][38] Proteomic analysis of the plasma membrane-tubular movement complexes of Cowpea mosaic virus (CPMV; Genus Comovirus) revealed that viral MPs, small and large CPs and RdRps colocalize with host-encoded PD-localized proteins as well as host ribosomes and tRNAs. 39 The cytoplasmic ends of tubules associated with Broad bean wilt virus 2 (BBWV2; Genus F I G U R E 1 Schematic illustrations of the architecture and intracellular distribution of TMV-, A, PVX-, B, and TuMV-induced inclusions, C. All elements are not drawn to scale Fabavirus) VP37 are always associated with membrane structures similar to those involved in virus replication. 40 The MP (also known as P1)…”

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confidence: 99%

Intercellular movement of plant RNA viruses: Targeting replication complexes to the plasmodesma for both accuracy and efficiency

Cheng

2020

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Replication and movement are two critical steps in plant virus infection. Recent advances in the understanding of the architecture and subcellular localization of virus-induced inclusions and the interactions between viral replication complex (VRC) and movement proteins (MPs) allow for the dissection of the intrinsic relationship between replication and movement, which has revealed that recruitment of VRCs to the plasmodesma (PD) via direct or indirect MP-VRC interactions is a common strategy used for cell-to-cell movement by most plant RNA viruses. In this review, we summarize the recent advances in the understanding of virus-induced inclusions and their roles in virus replication and cell-to-cell movement, analyze the advantages of such coreplicational movement from a viral point of view and discuss the possible mechanical force by which MPs drive the movement of virions or viral RNAs through the PD. Finally, we highlight the missing pieces of the puzzle of viral movement that are especially worth investigating in the near future.

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Proteomic analysis of the plasma membrane-movement tubule complex of cowpea mosaic virus

Cited by 5 publications

References 42 publications

The role of plasmodesma-located proteins in tubule-guided virus transport is limited to the plasmodesmata

The role of plasmodesma-located proteins in tubule-guided virus transport is limited to the plasmodesmata

The phosphorylation of the movement protein TGBp1 regulates the accumulation of the Bamboo mosaic virus

Intercellular movement of plant RNA viruses: Targeting replication complexes to the plasmodesma for both accuracy and efficiency

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