Structural Lability of Barley Stripe Mosaic Virus Virions

Makarov, Valentin V.; Скурат, Е.В.; Semenyuk, Pavel I.; Abashkin, Dmitry A.; Калинина, Н. В.; Arutyunyan, Alexander M.; Solovyev, Andrey G.; Добров, Е. Н.

doi:10.1371/journal.pone.0060942

Cited by 24 publications

(24 citation statements)

References 38 publications

(45 reference statements)

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“…Two lateral inter-subunit salt bridges are also present in TMV ( Figure 6 ), CGMMV, RMV, and HLSV, but the ion pairs forming them vary between the different viruses (TMV/RMV Arg113-Asp115 and Arg122-Asp88; CGMMV Arg113-Asp115 and Arg77-Glu130; HLSV His122-Asp88 and Arg31-Glu81) ( Tewary et al., 2011 ). It is possible that the reduced number of inter-subunit interactions in BSMV may explain its lower stability compared with TMV virions ( Makarov et al., 2013 ).…”

Section: Resultsmentioning

confidence: 99%

Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy

et al. 2015

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SummaryBarley stripe mosaic virus (BSMV, genus Hordeivirus) is a rod-shaped single-stranded RNA virus similar to viruses of the structurally characterized and well-studied genus Tobamovirus. Here we report the first high-resolution structure of BSMV at 4.1 Å obtained by cryo-electron microscopy. We discovered that BSMV forms two types of virion that differ in the number of coat protein (CP) subunits per turn and interactions between the CP subunits. While BSMV and tobacco mosaic virus CP subunits have a similar fold and interact with RNA using conserved residues, the axial contacts between the CP of these two viral groups are considerably different. BSMV CP subunits lack substantial axial contacts and are held together by a previously unobserved lateral contact formed at the virion surface via an interacting loop, which protrudes from the CP hydrophobic core to the adjacent CP subunit. These data provide an insight into diversity in structural organization of helical viruses.

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Section: Resultsmentioning

confidence: 99%

Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy

et al. 2015

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“…The TRV 16 K protein coding sequence was cloned into bacterial expression vector pQE32 (Qiagen, Hilden, Germany) to generate a construct with 16K tagged at the N terminus with 6xHis (16K-His). A construct expressing the plant 6xHis-coilin gene was generated previously (Makarov et al, 2013). Proteins were purified under denaturing conditions using Ni-NTA Qiagen agarose (Qiagen), according to the manufacturer's protocol.…”

Section: Expression and Purification Of The Recombinant Trv 16k Protementioning

confidence: 99%

Interaction of a plant virus protein with the signature Cajal body protein coilin facilitates salicylic acid‐mediated plant defence responses

et al. 2019

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Summary In addition to well‐known roles in RNA metabolism, the nucleolus and Cajal bodies (CBs), both located within the nucleus, are involved in plant responses to biotic and abiotic stress. Previously we showed that plants in which expression of the CB protein coilin is downregulated are more susceptible to certain viruses including tobacco rattle virus (TRV), suggesting a role of coilin in antiviral defence. Experiments with coilin‐deficient plants and the deletion mutant of the TRV 16K protein showed that both 16K and coilin are required for restriction of systemic TRV infection. The potential mechanisms of coilin‐mediated antiviral defence were elucidated via experiments involving co‐immunoprecipitation, use of NahG transgenic plants deficient in salicylic acid (SA) accumulation, measurement of endogenous SA concentrations and assessment of SA‐responsive gene expression. Here we show that TRV 16K interacts with and relocalizes coilin to the nucleolus. In wild‐type plants these events are accompanied by activation of SA‐responsive gene expression and restriction of TRV systemic infection. By contrast, viral systemic spread was enhanced in NahG plants, implicating SA in these processes. Our findings suggest that coilin is involved in plant defence, responding to TRV infection by recognition of the TRV‐encoded 16K protein and activating SA‐dependent defence pathways.

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“…These interactions are believed to determine the stability of tobamovirus virions, which is exceptionally high among helical plant viruses (Makarov et al, 2013).…”

Section: Strong Inter-subunit Interactions In Tobamovirus Virionsmentioning

confidence: 99%

“…In support of this view, the cryoelectron microscopy-based reconstruction of rod-shaped Barley stripe mosaic virus (BSMV, genus Hordeivirus) at a resolution of 19 Å revealed no drastic differences from TMV in the virion structure (Kendall et al, 2013). However, structural studies of the BSMV CP and virions employing analyses of circular dichroism spectra, differential scanning calorimetry and tryptophan spectra have demonstrated that the BSMV virions are considerably more labile than the TMV virions and, in general, the physicochemical characteristics of BSMV virions resemble those of flexuous filamentous viruses rather than TMV (Makarov et al, 2013). The recently reported high-resolution structure of BSMV at 4.1 Å obtained by cryoelectron microscopy (Protein Data Bank accession numbers 5a79 and 5a7a) provides an explanation for this contradiction (Clare et al, 2015).…”

Section: Intermediate Mode Of Subunit Interaction In Hordeivirus Capsidsmentioning

confidence: 99%

“…According to the data on physicochemical characteristics of virions (Makarov et al, 2013), salt bridges and other electrostatic interactions in the TMV virion provide even more stable inter-subunit contacts than the firm lateral contacts in hordeivirus virions. The TMV-like lateral contacts, based mainly on electrostatic interactions and devoid of any structural element for inter-subunit contacts on the outer surface of virions, appear to be unique for tobamoviruses.…”

Section: Cp Folds In Rod-shaped and Filamentous Viruses And Their Evomentioning

confidence: 99%

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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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Structural Lability of Barley Stripe Mosaic Virus Virions

Cited by 24 publications

References 38 publications

Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy

Novel Inter-Subunit Contacts in Barley Stripe Mosaic Virus Revealed by Cryo-Electron Microscopy

Interaction of a plant virus protein with the signature Cajal body protein coilin facilitates salicylic acid‐mediated plant defence responses

Helical capsids of plant viruses: architecture with structural lability

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