The Tobacco etch virus P3 protein forms mobile inclusions via the early secretory pathway and traffics along actin microfilaments

Cui, Xiaoyan; Wèi, Tàiyún; Chowda-Reddy, R. V.; Sun, Guangyu; Wang, Aiming

doi:10.1016/j.virol.2009.11.015

Cited by 74 publications

(74 citation statements)

References 68 publications

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“…Functional P3 protein was found to be recruited to the potyvirus replication complex (31) and to be involved in accumulation of the virus (32,33), symptomatology (34,35), viral microtubule-related inter-and intracellular movement (36), and determination of host range (33). Few examples of interaction of P3 with host factors have been reported.…”

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confidence: 99%

Quantitative and Qualitative Involvement of P3N-PIPO in Overcoming Recessive Resistance against Clover Yellow Vein Virus in Pea Carrying the cyv1 Gene

Choi

Hagiwara‐Komoda

Nakahara

et al. 2013

J Virol

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In pea carrying cyv1, a recessive gene for resistance to Clover yellow vein virus (ClYVV), ClYVV isolate Cl-no30 was restricted to the initially infected cells, whereas isolate 90-1 Br2 overcame this resistance. We mapped the region responsible for breaking of cyv1-mediated resistance by examining infection of cyv1 pea with chimeric viruses constructed from parts of Cl-no30 and 90-1 Br2. The breaking of resistance was attributed to the P3 cistron, which is known to produce two proteins: P3, from the main open reading frame (ORF), and P3N-PIPO, which has the N-terminal part of P3 fused to amino acids encoded by a small open reading frame (ORF) called PIPO in the ؉2 reading frame. We introduced point mutations that were synonymous with respect to the P3 protein but nonsynonymous with respect to the P3N-PIPO protein, and vice versa, into the chimeric viruses. Infection of plants with these mutant viruses revealed that both P3 and P3N-PIPO were involved in overcoming cyv1-mediated resistance. Moreover, P3N-PIPO quantitatively affected the virulence of Cl-no30 in cyv1 pea. Additional expression in trans of the P3N-PIPO derived from Cl-no30, using White clover mosaic virus as a vector, enabled Cl-no30 to move to systemic leaves in cyv1 pea. Susceptible pea plants infected with chimeric ClYVV possessing the P3 cistron of 90-1 Br2, and which were therefore virulent toward cyv1 pea, accumulated more P3N-PIPO than did those infected with Cl-no30, suggesting that the higher level of P3N-PIPO in infected cells contributed to the breaking of resistance by 90-1 Br2. This is the first report showing that P3N-PIPO is a virulence determinant in plants resistant to a potyvirus.

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confidence: 99%

Quantitative and Qualitative Involvement of P3N-PIPO in Overcoming Recessive Resistance against Clover Yellow Vein Virus in Pea Carrying the cyv1 Gene

Choi

Hagiwara‐Komoda

Nakahara

et al. 2013

J Virol

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“…Recent experiments showed that P3 is targeted to the membranes of the endoplasmic reticulum (ER) and forms inclusions associated with the Golgi apparatus that traffi c along the actin fi laments and colocalize with replication vesicles (Revers and Garcia, 2015). Two hydrophobic regions were identifi ed in the P3 of several potyviruses, and the one located in the C-terminal end of the protein was shown to be responsible for the ER targeting of P3 (Cui et al, 2010). Th is transmembrane domain is predicted to be located between residues 261 and 281.…”

Section: Genome Sequence Propertiesmentioning

confidence: 99%

Genome sequence of a divergent Colombian isolate of potato virus V (PVV) infecting Solanum phureja

Gutiérrez¹,

Hj²,

M³

2016

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Summary. -Deep sequencing analysis of the transcriptome of a Solanum phureja cv. Criolla Colombia plant with symptoms typical of a virus disease revealed an infection with potato virus V (PVV). Th e PVV-phureja genome comprises 9904 nt, exhibits 83% nucleotide identity with currently fully sequenced PVV isolates and contains one large ORF that codes for a polyprotein of 3065 residues fl anked by 5' and 3' UTR of 217 and 448 nt, respectively. Phylogenetic analysis of the PVV-phureja polyprotein indicates that it is divergent with respect to most PVV isolates. Th is is the fi rst complete PVV genome of an isolate infecting a host diff erent to S. tuberosum and, to this date, the only one from the South American Andes.

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“…Several viral proteins relevant to viral cell-to-cell movement hijack the actomyosin cytoskeleton to be targeted to plasmodesmata (11)(12)(13). In addition, a number of proteins and protein complexes not directly involved in cell-tocell movement have been shown to form motile inclusions and to traffic rapidly along the actin/ER network (14)(15)(16)(17)(18)(19)(20). One explanation for the motility of viral proteins is that they are anchored to, or in some cases vesiculated by, the endomembrane for the direct use of myosin motors, which provide the motive force (21,22).…”

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confidence: 99%

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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The Tobacco etch virus P3 protein forms mobile inclusions via the early secretory pathway and traffics along actin microfilaments

Cited by 74 publications

References 68 publications

Quantitative and Qualitative Involvement of P3N-PIPO in Overcoming Recessive Resistance against Clover Yellow Vein Virus in Pea Carrying the cyv1 Gene

Quantitative and Qualitative Involvement of P3N-PIPO in Overcoming Recessive Resistance against Clover Yellow Vein Virus in Pea Carrying the cyv1 Gene

Genome sequence of a divergent Colombian isolate of potato virus V (PVV) infecting Solanum phureja

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

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