Dual-colour imaging of membrane protein targeting directed by poa semilatent virus movement protein TGBp3 in plant and mammalian cells

Zamyatnin, Andrey A.; Solovyev, Andrey G.; Sablina, Anna; Agranovsky, Alexey A.; Katul, L.; Vetten, H. J.; Schiemann, Joachim; Hinkkanen, Ari; Lehto, Kirsi; Morozov, Sergey Y.

doi:10.1099/0022-1317-83-3-651

Cited by 54 publications

(71 citation statements)

References 93 publications

(130 reference statements)

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“…The above findings are in general agreement that the movement proteins of several viruses may associate with the endomembrane system (see Oparka, 2004) and are in line with the reported localization of TGB proteins of Poa semilatent hordeivirus (PSLV; Solovyev et al, 2000) and PVX Mitra et al, 2003), which in transient expression assays showed an association with the ER network or ER-derived structures at the cell periphery (Solovyev et al, 2000;Zamyatnin et al, 2002). Mutations in the predicted transmembrane domains of PVX TGB proteins that disrupt membrane binding inhibited the association with ER and virus movement Mitra et al, 2003).…”

Section: Introductionsupporting

confidence: 76%

“…Moreover, TGB proteins are expressed at low levels and are not readily detectable in virus-infected plants. Therefore, in several studies, the role and functions of TGB2 and TGB3 proteins have been investigated using microinjection or biolistic bombardment to introduce plasmids for transient expression of fluorescent fusion proteins (Solovyev et al, 2000;Zamyatnin et al, 2002Zamyatnin et al, , 2004Krishnamurthy et al, 2003;Mitra et al, 2003). In addition, expression of fusion proteins from viral vectors has provided (G) GFP-Ara7 labels vesicles throughout the cytoplasm of the cell, seen here near the cell periphery (arrow) (green channel).…”

Section: Discussionmentioning

confidence: 99%

“…In studies with PSLV, coexpression of the two proteins revealed that they colocalized in the cell and that TGB3 redirected localization of TGB2 from the ER network to the peripheral bodies (Solovyev et al, 2000). TGB3-assisted targeting to the periphery has also been shown with unrelated proteins, such as PVX TGB2 and the 6-kD movement protein of Beet yellows closterovirus (Solovyev et al, 2000;Zamyatnin et al, 2002). Also, evidence for the association of PSLV TGB3 with plasmodesmata has been obtained from experiments with GFP-TGB3 transgenic plants in which colocalization with callose deposits was observed (Gorshkova et al, 2003).…”

Section: Introductionmentioning

confidence: 96%

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Two Plant–Viral Movement Proteins Traffic in the Endocytic Recycling Pathway

Haupt¹,

Cowan²,

Ziegler³

et al. 2005

The Plant Cell

194

157

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Many plant viruses exploit a conserved group of proteins known as the triple gene block (TGB) for cell-to-cell movement. Here, we investigated the interaction of two TGB proteins (TGB2 and TGB3) of Potato mop-top virus (PMTV), with components of the secretory and endocytic pathways when expressed as N-terminal fusions to green fluorescent protein or monomeric red fluorescent protein (mRFP). Our studies revealed that fluorophore-labeled TGB2 and TGB3 showed an early association with the endoplasmic reticulum (ER) and colocalized in motile granules that used the ER-actin network for intracellular movement. Both proteins increased the size exclusion limit of plasmodesmata, and TGB3 accumulated at plasmodesmata in the absence of TGB2. TGB3 contains a putative Tyr-based sorting motif, mutations in which abolished ER localization and plasmodesmatal targeting. Later in the expression cycle, both fusion proteins were incorporated into vesicular structures. TGB2 associated with these structures on its own, but TGB3 could not be incorporated into the vesicles in the absence of TGB2. Moreover, in addition to localization to the ER and motile granules, mRFP-TGB3 was incorporated into vesicles when expressed in PMTV-infected epidermal cells, indicating recruitment by virus-expressed TGB2. The TGB fusion protein-containing vesicles were labeled with FM4-64, a marker for plasma membrane internalization and components of the endocytic pathway. TGB2 also colocalized in vesicles with Ara7, a Rab5 ortholog that marks the early endosome. Protein interaction analysis revealed that recombinant TGB2 interacted with a tobacco protein belonging to the highly conserved RME-8 family of J-domain chaperones, shown to be essential for endocytic trafficking in Caenorhabditis elegans and Drosophila melanogaster. Collectively, the data indicate the involvement of the endocytic pathway in viral intracellular movement, the implications of which are discussed.

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Section: Introductionsupporting

confidence: 76%

Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

See 1 more Smart Citation

Two Plant–Viral Movement Proteins Traffic in the Endocytic Recycling Pathway

Haupt¹,

Cowan²,

Ziegler³

et al. 2005

The Plant Cell

194

157

View full text Add to dashboard Cite

show abstract

“…It is possible that TGBp2 can direct TGBp3 to the same ER vesicles during viral infection. Studies prove that TGBp2 and TGBp3 sometimes coexist (Zamyatnin et al 2002). So far there has not been provided any data which would show whether TGBp2-related vesicles contain TGBp1, vRNA, CP or virus-like particles.…”

Section: Tgb Cooperating Systemmentioning

confidence: 99%

Cell-to-cell movement of three genera (+) ss RNA plant viruses

Otulak

Garbaczewska

2010

Acta Physiol Plant

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The current investigations of three genera plant virus cell-to-cell movement were presented. Viruses reveal different local transport strategies, but all of them are the results of virus factors-host components interactions. The Tobacco mosaic virus (TMV) does not require capsid protein for translocation through plasmodesmata but 30 K movement protein participates in this process. It was found direct or indirect TMV movement proteins host partners in Tobamovirus movement like: pectin methylesterase, movement protein binding 2C, chaperones or cytoskeleton components and endoplasmatic reticulum membranes. The Potex-and Potyvirus cell-to-cell movement is closely related to replication network. The PVX capsid protein and triple gene block protein system are responsible for efficient local transport. Potyviruses move through the plasmodesmata by involving viral encoded proteins but not specific movement proteins. While the Potyvirus is the biggest known plant virus genus, host components participating in or regulating directly its plasmodesmata-movement are still not clear.

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“…En lo que respecta a las proteínas TGBp2 y TGBp3, son productos de menor tamaño y funcionan como proteínas integrales de membrana en ambas clases de virus [Tamai & Meshi, 2001;Cowan et al, 2002;Zamyatnin et al, 2002;Krishnamurthy et al, 2003;Gorshkova et al, 2003]. El producto TGBp2, cuyo tamaño oscila entre 11-14 kDa, posee dos secuencias hidrofóbicas internas que median su inserción en RE, dejando la región intermedia hidrofílica, muy conservada, dispuesta a modo de lazo hacia la cara luminal del orgánulo y los extremos N-t y C-t expuestos al citoplasma [Zamyatnin et al, 2006;Hsu et al, 2008;Lee et al, 2010].…”

Section: Bloque Triple De Genesunclassified

Análisis Funcional De Proteínas Codificadas Por El Virus De La Rotura Del Color De La Flor Del Pelargonium

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Dual-colour imaging of membrane protein targeting directed by poa semilatent virus movement protein TGBp3 in plant and mammalian cells

Cited by 54 publications

References 93 publications

Two Plant–Viral Movement Proteins Traffic in the Endocytic Recycling Pathway

Two Plant–Viral Movement Proteins Traffic in the Endocytic Recycling Pathway

Cell-to-cell movement of three genera (+) ss RNA plant viruses

Análisis Funcional De Proteínas Codificadas Por El Virus De La Rotura Del Color De La Flor Del Pelargonium

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