Negative-strand RNA viruses: The plant-infecting counterparts

Kormelink, Richard; García, María Laura; Goodin, Michael M.; Sasaya, Takahide; Haenni, Anne‐Lise

doi:10.1016/j.virusres.2011.09.028

Cited by 167 publications

(181 citation statements)

References 159 publications

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“…An H74L mutation was introduced into Sar1 by using the GeneArt seamless cloning and assembly kit (Invitrogen), and the Sar1(H74L) gene was cloned into pEarleyGate 100. An FABD2 sequence (At4G26700) and all myosin tail sequences (XI-1 [AT1G17580]; XI-2 [AT5G43900]; XI-J [AT3G58160]; XI-K [AT5G20490]) were amplified from cDNA derived from A. thaliana (25,38) and cloned into pEarleyGate 104 and pEarleyGate NCFP, an in-house expression vector built from pEarleyGate 104 to introduce cyan fluorescent protein (CFP) as an N-terminal fusion. The CFP sequence containing a simian virus 40 (SV40) nuclear localization signal (NLS) sequence was amplified using a primer containing an NLS sequence (39) and cloned into pEarleyGate 100.…”

Section: Construction Of Binary Vectorsmentioning

confidence: 99%

“…Although NPs are characterized by their general RNA-binding activities (25,29), NPs of emaraviruses, including FMV, had not been assessed for RNAbinding activity. RNA-binding activity was verified in an EMSA using a recombinant fusion of NP with maltose-binding protein (MBP:NP).…”

Section: Np Formed Agglomerates That Were Enveloped By the Er Membranmentioning

confidence: 99%

“…Negative-sense single-stranded RNA [(-)RNA] viruses induce the modification of intracellular membrane structures to form membrane-enveloped particles (23)(24)(25)(26). Glycoprotein (GP), a structural protein encoded by (-)RNA viruses, targets specific organelles and hijacks the membrane to enclose viral ribonucleoprotein complexes (vRNPs), which play key roles in viral replication and translation.…”

mentioning

confidence: 99%

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Nucleocapsid Protein from Fig Mosaic Virus Forms Cytoplasmic Agglomerates That Are Hauled by Endoplasmic Reticulum Streaming

Ishikawa

Miura

Maejima

et al. 2015

J Virol

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Although many studies have demonstrated intracellular movement of viral proteins or viral replication complexes, little is known about the mechanisms of their motility. In this study, we analyzed the localization and motility of the nucleocapsid protein (NP) of Fig mosaic virus (FMV), a negative-strand RNA virus belonging to the recently established genus Emaravirus. Electron microscopy of FMV-infected cells using immunogold labeling showed that NPs formed cytoplasmic agglomerates that were predominantly enveloped by the endoplasmic reticulum (ER) membrane, while nonenveloped NP agglomerates also localized along the ER. Likewise, transiently expressed NPs formed agglomerates, designated NP bodies (NBs), in close proximity to the ER, as was the case in FMV-infected cells. Subcellular fractionation and electron microscopic analyses of NP-expressing cells revealed that NBs localized in the cytoplasm. Furthermore, we found that NBs moved rapidly with the streaming of the ER in an actomyosin-dependent manner. Brefeldin A treatment at a high concentration to disturb the ER network configuration induced aberrant accumulation of NBs in the perinuclear region, indicating that the ER network configuration is related to NB localization. Dominant negative inhibition of the class XI myosins, XI-1, XI-2, and XI-K, affected both ER streaming and NB movement in a similar pattern. Taken together, these results showed that NBs localize in the cytoplasm but in close proximity to the ER membrane to form enveloped particles and that this causes passive movements of cytoplasmic NBs by ER streaming. IMPORTANCEIntracellular trafficking is a primary and essential step for the cell-to-cell movement of viruses. To date, many studies have demonstrated the rapid intracellular movement of viral factors but have failed to provide evidence for the mechanism or biological significance of this motility. Here, we observed that agglomerates of nucleocapsid protein (NP) moved rapidly throughout the cell, and we performed live imaging and ultrastructural analysis to identify the mechanism of motility. We provide evidence that cytoplasmic protein agglomerates were passively dragged by actomyosin-mediated streaming of the endoplasmic reticulum (ER) in plant cells. In virus-infected cells, NP agglomerates were surrounded by the ER membranes, indicating that NP agglomerates form the basis of enveloped virus particles in close proximity to the ER. Our work provides a sophisticated model of macromolecular trafficking in plant cells and improves our understanding of the formation of enveloped particles of negative-strand RNA viruses.T he actomyosin system is essential for the intracellular transport of endomembranes and other macromolecular complexes and for the spatial arrangement of organelles (1). Trafficking along actin filaments is primarily mediated by molecular motor myosins. Myosins of Arabidopsis thaliana are divided into the two subfamilies, class VIII and class XI myosins. Class XI myosins provide the motive force for the movement of org...

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Section: Construction Of Binary Vectorsmentioning

confidence: 99%

Section: Np Formed Agglomerates That Were Enveloped By the Er Membranmentioning

confidence: 99%

mentioning

confidence: 99%

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Nucleocapsid Protein from Fig Mosaic Virus Forms Cytoplasmic Agglomerates That Are Hauled by Endoplasmic Reticulum Streaming

Ishikawa

Miura

Maejima

et al. 2015

J Virol

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“…umerous viruses infecting plants are classified as rhabdoviruses most generally on the basis of electron microscopic observations of distinctive enveloped bacilliform or bullet-shaped particles in the infected cells (1,2). Only a few of them were confirmed to be true rhabdoviruses by sequencing of their genome and molecular studies (1,2).…”

mentioning

confidence: 99%

“…Only a few of them were confirmed to be true rhabdoviruses by sequencing of their genome and molecular studies (1,2). The Rhabdoviridae belong to the nonsegmented negative-stranded RNA viruses (NNVs); together with the Paramyxoviridae, the Filoviridae, and the Bornaviridae, they constitute the order Mononegavirales.…”

mentioning

confidence: 99%

Structure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus Phosphoprotein

Martínez

Ribeiro

Leyrat

et al. 2013

J Virol

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e Lettuce necrotic yellows virus (LNYV) is a prototype of the plant-adapted cytorhabdoviruses. Through a meta-prediction of disorder, we localized a folded C-terminal domain in the amino acid sequence of its phosphoprotein. This domain consists of an autonomous folding unit that is monomeric in solution. Its structure, solved by X-ray crystallography, reveals a lollipop-shaped structure comprising five helices. The structure is different from that of the corresponding domains of other Rhabdoviridae, Filoviridae, and Paramyxovirinae; only the overall topology of the polypeptide chain seems to be conserved, suggesting that this domain evolved under weak selective pressure and varied in size by the acquisition or loss of functional modules.

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Multi‐component Plant Viruses

Zhang

2015

Encyclopedia of Life Sciences

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Many plant viruses divide their coding capacity into multiple genomic segments, hence are referred to as multi‐component viruses. These include viruses with either RNA or DNA genomes, in either single‐stranded (ss) or double‐stranded (ds) conformations. Furthermore, those with ssRNA genomes may encode viral proteins on the genome strand ([+] sense RNA viruses), the complementary strand ([−] sense RNA viruses) of the genomic RNA or both (ambisense RNA viruses). Multi‐component, (+) sense RNA viruses could comprise up to five genome segments, whereas (−) sense RNA viruses can have up to eight. Strikingly, most of characterised dsRNA viruses have 10–12 genome segments packaged in the same virus particles. Finally, the genomes of multi‐component DNA plant viruses are almost always single‐stranded, circular, and each of the segments (up to eight) is packaged in separate particles. Possible evolutionary relationships between multi‐component viruses and their monopartite relatives are discussed. Key Concepts Plant virus genomes can be non‐segmented (monopartite) or segmented (multi‐partite). Multi‐partite plant viruses can be found in almost all major plant virus families, with different genome materials (RNA or DNA) and configurations (single‐stranded or double‐stranded), and varying virion shapes. Plant viruses with most genome segments are plant‐infecting reoviruses, containing 10–12 double‐stranded RNA segments package together in the same non‐enveloped, multi‐layer capsids. Nanoviruses are small viruses with up to eight single‐stranded, circular DNA genomes separately packaged in isometric particles.

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Negative-strand RNA viruses: The plant-infecting counterparts

Cited by 167 publications

References 159 publications

Nucleocapsid Protein from Fig Mosaic Virus Forms Cytoplasmic Agglomerates That Are Hauled by Endoplasmic Reticulum Streaming

Nucleocapsid Protein from Fig Mosaic Virus Forms Cytoplasmic Agglomerates That Are Hauled by Endoplasmic Reticulum Streaming

Structure of the C-Terminal Domain of Lettuce Necrotic Yellows Virus Phosphoprotein

Multi‐component Plant Viruses

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