Complex molecular architecture of beet yellows virus particles

Peremyslov, Valera V.; Андреев, И. А.; Prokhnevsky, Alexey I.; Duncan, G. H.; Taliansky, Michael; Dolja, Valerian V.

doi:10.1073/pnas.0400303101

Cited by 83 publications

(75 citation statements)

References 45 publications

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“…The TGB MPs are involved in multiple interactions between themselves (18,38), while tubule-forming MPs enclose virions into the tubes formed during infection (29). In addition to accumulation in PDs, BYV Hsp70h is incorporated to virion tails that function in virus transport (2,36,42,47,53).…”

Section: Discussionmentioning

confidence: 99%

“…Strikingly, each of these four proteins is an integral component of the ϳ1,400-nm-long filamentous virions with CP coating ϳ97% of the 15.5 kb RNA genome. The remaining three proteins, CPm, p64, and Hsp70h, assemble a ϳ100-nm-long tail that encapsidates a 5Ј-terminal, ϳ600-nucleotide (nt)-long RNA segment (47). An additional, 20-kDa, tail protein is not required for the cell-to-cell movement, but is essential for the viral transport through the phloem (53).…”

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confidence: 99%

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Actin Cytoskeleton Is Involved in Targeting of a Viral Hsp70 Homolog to the Cell Periphery

Prokhnevsky

Peremyslov

Dolja

2005

J Virol

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The cell-to-cell movement of plant viruses involves translocation of virus particles or nucleoproteins to and through the plasmodesmata (PDs). As we have shown previously, the movement of the Beet yellows virus requires the concerted action of five viral proteins including a homolog of cellular ϳ70-kDa heat shock proteins (Hsp70h). Hsp70h is an integral component of the virus particles and is also found in PDs of the infected cells. Here we investigate subcellular distribution of Hsp70h using transient expression of Hsp70h fused to three spectrally distinct fluorescent proteins. We found that fluorophore-tagged Hsp70h forms motile granules that are associated with actin microfilaments, but not with microtubules. In addition, immobile granules were observed at the cell periphery. A pairwise appearance of these granules at the opposite sides of cell walls and their colocalization with the movement protein of Tobacco mosaic virus indicated an association of Hsp70h with PDs. Treatment with various cytoskeleton-specific drugs revealed that the intact actomyosin motility system is required for trafficking of Hsp70h in cytosol and its targeting to PDs. In contrast, none of the drugs interfered with the PD localization of Tobacco mosaic virus movement protein. Collectively, these findings suggest that Hsp70h is translocated and anchored to PDs in association with the actin cytoskeleton.

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Section: Discussionmentioning

confidence: 99%

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confidence: 99%

Actin Cytoskeleton Is Involved in Targeting of a Viral Hsp70 Homolog to the Cell Periphery

Prokhnevsky

Peremyslov

Dolja

2005

J Virol

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“…Although the other three recombinant capsid components do not bind specifically to the whitefly vector, we cannot rule out the possibility that, in the context of the assembled virion, they may have some yet unknown functions associated with virus transmission. Because the CPm, CP, HSP70h, and P59 are interacting capsid components (11,33,34), it is intriguing that in the absence of a complete CPm, the agropR6-5b mutant is still capable of systemic plant infection and encapsidation, perhaps by one or more of the other three components compensating for the truncated CPm (10). However, it is clear from our data that virion retention and transmission by vectors are dependent on the presence of a complete CPm and cannot be substituted or compensated for.…”

Section: Discussionmentioning

confidence: 99%

A virus capsid component mediates virion retention and transmission by its insect vector

Chen¹,

Walker²,

Carter

et al. 2011

Proc. Natl. Acad. Sci. U.S.A.

104

119

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Numerous pathogens of humans, animals, and plants are transmitted by specific arthropod vectors. However, understanding the mechanisms governing these pathogen-vector interactions is hampered, in part, by the lack of easy-to-use analytical tools. We investigated whitefly transmission of Lettuce infectious yellows virus (LIYV) by using a unique immunofluorescent localization approach in which we fed virions or recombinant virus capsid components to whiteflies, followed by feeding them antibodies to the virions or capsid components, respectively. Fluorescent signals, indicating the retention of virions, were localized in the anterior foregut or cibarium of a whitefly vector biotype but not within those of a whitefly nonvector biotype. Retention of virions in these locations strongly corresponded with the whitefly vector transmission of LIYV. When four recombinant LIYV capsid components were individually fed to whitefly vectors, significantly more whiteflies retained the recombinant minor coat protein (CPm). As demonstrated previously and in the present study, whitefly vectors failed to transmit virions preincubated with anti-CPm antibodies but transmitted virions preincubated with antibodies recognizing the major coat protein (CP). Correspondingly, the number of insects that specifically retained virions preincubated with antiCPm antibodies were significantly reduced compared with those that specifically retained virions preincubated with anti-CP antibodies. Notably, a transmission-defective CPm mutant was deficient in specific virion retention, whereas the CPm-restored virus showed WT levels of specific virion retention and transmission. These data provide strong evidence that transmission of LIYV is determined by a CPm-mediated virion retention mechanism in the anterior foregut or cibarium of whitefly vectors.arthropod vector transmission | crinivirus | noncirculative transmission | semipersistent transmission | Bemisia tabaci

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“…The latter is dispensable for virion formation and virus cell-to-cell movement, but is essential for the viral systemic transport through the plant vascular system (Prokhnevsky et al, 2002). 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 .…”

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

confidence: 99%

“…The main virion part (approximately 95 % of its length) is made of the CP, while the remaining segment, which is located at the virion end encapsidating the 5¢-terminal region of genomic RNA, is formed by the CPm (Agranovsky et al, 1995;Peremyslov et al, 2004;Satyanarayana et al, 2004). Additionally, the CPm-formed region of BYV virions contains three other viral proteins, namely an Hsp70 homologue (Hsp70h), a p64 protein with a CP-like structural domain in its C-terminal region and p20 (Kiss et al, 2013;Napuli et al, 2000Napuli et al, , 2003Tian et al, 1999).…”

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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Complex molecular architecture of beet yellows virus particles

Cited by 83 publications

References 45 publications

Actin Cytoskeleton Is Involved in Targeting of a Viral Hsp70 Homolog to the Cell Periphery

Actin Cytoskeleton Is Involved in Targeting of a Viral Hsp70 Homolog to the Cell Periphery

A virus capsid component mediates virion retention and transmission by its insect vector

Helical capsids of plant viruses: architecture with structural lability

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