Formation of protein complexes containing plant virus movement protein TGBp3 is necessary for its intracellular trafficking

Shemyakina, Elena A.; Erokhina, Tatiana N.; Gorshkova, Elena N.; Schiemann, Joachim; Solovyev, Andrey G.; Morozov, Sergey Y.

doi:10.1016/j.biochi.2011.01.002

Cited by 17 publications

(22 citation statements)

References 49 publications

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“…The TGB3 proteins were shown to be expressed at very low levels in virus-infected tissues Shemyakina et al, 2011). Moreover, TGB3 proteins expressed at higher levels negatively affect subcellular transport of other TGB proteins to plasmodesmata or viral movement (Lauber et al, 2005), and cause severe structural rearrangements of the endoplasmic reticulum in plant cells .…”

Section: Translation Of Shvx Tgb3mentioning

confidence: 99%

Translation of the shallot virus X TGB3 gene depends on non-AUG initiation and leaky scanning

Lezzhov

Gushchin

Lazareva

et al. 2015

Journal of General Virology

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Triple gene block (TGB), a conserved gene module found in the genomes of many filamentous and rod-shaped plant viruses, encodes three proteins, TGB1, TGB2 and TGB3, required for viral cell-to-cell movement through plasmodesmata and systemic transport via the phloem. The genome of Shallot virus X, the type species of the genus Allexivirus, includes TGB1 and TGB2 genes, but contains no canonical ORF for TGB3 protein. However, a TGB3-like proteinencoding sequence lacking an AUG initiator codon has been found in the shallot virus X (ShVX) genome in a position typical for TGB3 genes. This putative TGB3 gene is conserved in all allexiviruses. Here, we carried out sequence analysis to predict possible non-AUG initiator codons in the ShVX TGB3-encoding sequence. We further used an agroinfiltration assay in Nicotiana benthamiana to confirm this prediction. Site-directed mutagenesis was used to demonstrate that the ShVX TGB3 could be translated on a bicistronic mRNA template via a leaky scanning mechanism.

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Section: Translation Of Shvx Tgb3mentioning

confidence: 99%

Translation of the shallot virus X TGB3 gene depends on non-AUG initiation and leaky scanning

Lezzhov

Gushchin

Lazareva

et al. 2015

Journal of General Virology

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“…TGBp3 plays an important role in intracellular viral movement by targeting the viral ribonucleoprotein complex to plasmodesmata for cell-to-cell movement (15). However, the relative abundance of TGBp3 is the lowest among the TGB proteins in infected cells, which makes it difficult to detect (27,29,30,32,51). Indeed, PMTV TGBp3 has previously been detected in infected leaf tissues only following overexpression from a heterologous viral vector (24).…”

Section: Discussionmentioning

confidence: 99%

“…Previous studies on PMTV TGBp3 have been done by producing the protein from a plant expression vector or heterologous virus (e.g., see references [23][24][25]. Indeed, the TGBp3 proteins present in infected plant tissues are extremely difficult to detect due to a low titer (26,29,31,32), and previous attempts to detect and localize PMTV TGBp3 in PMTV-infected plants have been unsuccessful (24). Hence, unequivocal evidence that TGBp3 of PMTV is expressed during virus infection remains to be obtained.…”

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confidence: 99%

Tyrosine Phosphorylation of the Triple Gene Block Protein 3 Regulates Cell-to-Cell Movement and Protein Interactions of Potato Mop-Top Virus

Samuilova

Santala

Valkonen

2013

J Virol

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Functions of viral proteins can be regulated through phosphorylation by serine/threonine kinases in plants, but little is known about the involvement of tyrosine kinases in plant virus infection. In this study, TGBp3, one of the three movement proteins encoded by a triple gene block (TGB) of Potato mop-top virus (PMTV), was detected for the first time in PMTV-infected plants and found to be tyrosine phosphorylated. Phosphorylation sites (Tyr 87-89 and Tyr 120 ) were located in two amino acid motifs conserved in the TGB-containing, rod-shaped plant viruses. Substitution of these tyrosine residues in both motifs was needed to abolish tyrosine phosphorylation of TGBp3. Substitution of Tyr 87-89 with alanine residues enhanced the interaction between TGBp3 and TGBp2 and inhibited cell-to-cell movement of PMTV. On the other hand, substitution of Tyr 120 with alanine resulted in no alteration in the interaction of TGBp3 with TGBp2, but the mutant virus was not infectious. The results suggest that tyrosine phosphorylation is a mechanism regulating the functions of plant virus movement proteins.

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“…Deletion analysis of hordeivirus TGBp3 reveals that the signal of plasmodesmata targeting is composite and consists of at least two parts, the central hydrophilic region containing an invariant pentapeptide YQDLN and the C-terminal transmembrane domain [10]. Recently, we have demonstrated that the YQDLN-containing conserved region is essential for TGBp3 incorporation into high-molecular-mass protein complexes representing the form in which TGBp3 is found in virus-infected plants [12]. Most importantly, the formation of such complexes is necessary for entering the TGBp3-specific pathway of intracellular transport and protein delivery to PMBs.…”

Section: Introductionmentioning

confidence: 99%

“…Most importantly, the formation of such complexes is necessary for entering the TGBp3-specific pathway of intracellular transport and protein delivery to PMBs. On the other hand, the C-terminal transmembrane segment is a bona fide signal of TGBp3 intracellular transport since the transport to PMBs of the protein with disabled YQDLN-containing region is restored by fusion to a heterologous peptide capable of multimer formation [12]. …”

Section: Introductionmentioning

confidence: 99%

Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression ofPoa semilatent virusMovement Protein

Solovyev

Schiemann²,

Morozov³

2012

The Scientific World Journal

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Cell-to-cell transport of plant viruses is mediated by virus-encoded movement proteins and occurs through plasmodesmata interconnecting neighboring cells in plant tissues. Three movement proteins coded by the “triple gene block” (TGB) and named TGBp1, TGBp2 and TGBp3 have distinct functions in viral transport. TGBp1 binds viral genomic RNAs to form ribonucleoprotein complexes representing the transport form of viral genome, while TGBp2 and TGBp3 are necessary for intracellular delivery of such complexes to plasmodesmata. Recently, it was revealed that overexpression of Potato virus X TGBp3 triggers the unfolded protein response mitigating the endoplasmic reticulum (ER) stress leading to cell death if this protein reaches high levels in the ER. Here we report microscopic studies of the influence of the Poa semilatent hordeivirus TGBp3 overexpressed in Nicotiana benthamiana epidermal cells by particle bombardment on cell endomembranes and demonstrate that the protein C-terminal transmembrane segment contains a determinant responsible for vesiculation and coalescence of the endoplasmic reticulum and Golgi presumably accompanying the ER stress that can be induced upon high-level TGBp3 expression.

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Formation of protein complexes containing plant virus movement protein TGBp3 is necessary for its intracellular trafficking

Cited by 17 publications

References 49 publications

Translation of the shallot virus X TGB3 gene depends on non-AUG initiation and leaky scanning

Translation of the shallot virus X TGB3 gene depends on non-AUG initiation and leaky scanning

Tyrosine Phosphorylation of the Triple Gene Block Protein 3 Regulates Cell-to-Cell Movement and Protein Interactions of Potato Mop-Top Virus

Microscopic Analysis of Severe Structural Rearrangements of the Plant Endoplasmic Reticulum and Golgi Caused by Overexpression ofPoa semilatent virusMovement Protein

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