Genetic Analysis of the Cell-to-Cell Movement of Beet Yellows Closterovirus

Alzhanova, Dina; Hagiwara, Yuka; Peremyslov, Valery V.; Dolja, Valerian V.

doi:10.1006/viro.1999.0155

Cited by 108 publications

(107 citation statements)

References 78 publications

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“…What is the primary function of p20 in the BYV life cycle? Previous work demonstrated that p20 is dispensable for BYV replication (39) and is not essential for virus cell-to-cell movement, although it might have an accessory role in the latter process (2). The interaction of p20 with Hsp70h, which is one of the three BYV MPs (40), prompted us to revisit the role of p20 in cell-to-cell movement.…”

Section: Resultsmentioning

confidence: 99%

Interaction between Long-Distance Transport Factor and Hsp70-Related Movement Protein of Beet Yellows Virus

Prokhnevsky

Peremyslov

Napuli

et al. 2002

J Virol

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110

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Systemic spread of viruses in plants involves local movement from cell to cell and long-distance transport through the vascular system. The cell-to-cell movement of the Beet yellows virus (BYV) is mediated by a movement protein that is an Hsp70 homolog (Hsp70h). This protein is required for the assembly of movementcompetent virions that incorporate Hsp70h. By using the yeast two-hybrid system, in vitro coimmunoprecipitation, and in planta coexpression approaches, we show here that the Hsp70h interacts with a 20-kDa BYV protein (p20). We further demonstrate that p20 is associated with the virions presumably via binding to Hsp70h. Genetic and immunochemical analyses indicate that p20 is dispensable for assembly and cell-to-cell movement of BYV but is required for the long-distance transport of virus through the phloem. These results reveal a novel activity for the Hsp70h that provides a molecular link between the local and systemic spread of a plant virus by docking a long-distance transport factor to virions.

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Section: Resultsmentioning

confidence: 99%

Interaction between Long-Distance Transport Factor and Hsp70-Related Movement Protein of Beet Yellows Virus

Prokhnevsky

Peremyslov

Napuli

et al. 2002

J Virol

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110

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“…Among the sequences available in protein databases, the corresponding protein of LIYV is the most similar (29.8% amino acid identity) to SPCSV p60. The CTV p61 protein, which corresponds to SPCSV p60, is essential for viral cell-to-cell movement (5) and virion assembly (55).…”

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confidence: 99%

“…However, the SPCSV CPm was 1.5-fold larger than that of LIYV (52 kDa), due primarily to differences within the N-proximal portions of the proteins. Studies of clostero-and crinivirus particles have revealed that CPm assembles within a 75-to 85-nm stretch at one end of the virus particle (3,21,58,66) and is essential for viral cell-to-cell movement (5,6). LIYV CPm has been implicated in virus transmissibility with the whitefly vector (58).…”

mentioning

confidence: 99%

Complete Genome Sequence and Analyses of the Subgenomic RNAs of Sweet Potato Chlorotic Stunt Virus Reveal Several New Features for the Genus Crinivirus

Kreuze

Savenkov

Valkonen

2002

J Virol

100

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The complete nucleotide sequences of genomic RNA1 (9,407 nucleotides [nt]) and RNA2 (8,223 nt) of Sweet potato chlorotic stunt virus (SPCSV; genus Crinivirus, family Closteroviridae) were determined, revealing that SPCSV possesses the second largest identified positive-strand single-stranded RNA genome among plant viruses after Citrus tristeza virus. RNA1 contains two overlapping open reading frames (ORFs) that encode the replication module, consisting of the putative papain-like cysteine proteinase, methyltransferase, helicase, and polymerase domains. RNA2 contains the Closteroviridae hallmark gene array represented by a heat shock protein homologue (Hsp70h), a protein of 50 to 60 kDa depending on the virus, the major coat protein, and a divergent copy of the coat protein. This grouping resembles the genome organization of Lettuce infectious yellows virus (LIYV), the only other crinivirus for which the whole genomic sequence is available. However, in striking contrast to LIYV, the two genomic RNAs of SPCSV contained nearly identical 208-nt-long 3 terminal sequences, and the ORF for a putative small hydrophobic protein present in LIYV RNA2 was found at a novel position in SPCSV RNA1. Furthermore, unlike any other plant or animal virus, SPCSV carried an ORF for a putative RNase III-like protein (ORF2 on RNA1). Several subgenomic RNAs (sgRNAs) were detected in SPCSV-infected plants, indicating that the sgRNAs formed from RNA1 accumulated earlier in infection than those of RNA2. The 5 ends of seven sgRNAs were cloned and sequenced by an approach that provided compelling evidence that the sgRNAs are capped in infected plants, a novel finding for members of the Closteroviridae.

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“…Atomic force microscopy studies demonstrate that the closterovirus virion terminal structure has a complex morphology and consists of three distinct segments, of which the tip segment is likely to be formed by the p20 protein (Peremyslov et al, 2004). Since the CPm, Hsp70h and p64 proteins are required for BYV cell-to-cell movement (Alzhanova et al, 2000;Peremyslov et al, 1999;Prokhnevsky et al, 2002), it has been concluded that the terminal structure represents the specialized device evolved to facilitate translocation of closterovirus virions to and through plasmodesmata . Of these proteins, Hsp70h may be the key element of BYV transport machinery, since this protein, when expressed in the absence of other viral products, is able to localize to motile granules, which are transported to the cell periphery in an actin-dependent manner, and can associate with plasmodesmata (Prokhnevsky et al, 2005).…”

Section: Role Of Virions In Cell-to-cell Transport Of Filamentous Virmentioning

confidence: 99%

Helical capsids of plant viruses: architecture with structural lability

Solovyev

Makarov

2016

Journal of General Virology

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Capsids of numerous filamentous and rod-shaped plant viruses possess helical symmetry. In positive-stranded RNA viruses, helical capsids are typically composed of many identical subunits of the viral capsid protein (CP), encapsidating a molecule of viral genomic RNA. Current progress in structural studies of helical plant viruses has revealed differences between filamentous and rod-shaped viruses, both in structural folds of their CPs and in the interactions of CP molecules in their capsids. Many filamentous and rod-shaped viruses have functionally similar lateral inter-subunit contacts on the outer virion surface. Additionally, the extreme Nterminal CP region in filamentous viruses is intrinsically disordered. Taken together, the available data establish a link between the structural features of molecular interactions of CP molecules and the physical properties of helical virions ranging from rigidity to flexibility. Overall, the structure of helical plant viruses is significantly more labile than previously thought, often allowing structural transitions, remodelling and the existence of alternative structural forms of virions. These properties of virions are believed to be functionally significant at certain stages of the viral life cycle, such as during translational activation and cell-to-cell transport. In this review, we discuss structural and functional features of filamentous and rod-shaped virions, highlight their shared features and differences, and lay emphasis on the relationships between the molecular structure of viral capsids and their properties including virion shape, lability and capability of structural remodelling.

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Genetic Analysis of the Cell-to-Cell Movement of Beet Yellows Closterovirus

Cited by 108 publications

References 78 publications

Interaction between Long-Distance Transport Factor and Hsp70-Related Movement Protein of Beet Yellows Virus

Interaction between Long-Distance Transport Factor and Hsp70-Related Movement Protein of Beet Yellows Virus

Complete Genome Sequence and Analyses of the Subgenomic RNAs of Sweet Potato Chlorotic Stunt Virus Reveal Several New Features for the Genus Crinivirus

Helical capsids of plant viruses: architecture with structural lability

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