The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses

Agirrezabala, Xabier; Méndez-López, Eduardo; Lasso, Gorka; Sánchez-Pina, M. Amelia; Aranda, Miguel A.; Valle, Mikel

doi:10.7554/elife.11795

Cited by 63 publications

(96 citation statements)

References 33 publications

(62 reference statements)

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“…In 2012, X-ray analysis of the CP expressed in bacteria along with cryoelectron microscopy of virions revealed the Papaya mosaic virus (PapMV) CP tertiary structure, which appeared to be distant from known folds of other plant viruses (Yang et al, 2012). In 2015, the structure of two other potexviruses was resolved at high resolution by cryoelectron microscopy, which shed new light on the details of intersubunit interactions in filamentous virions (Agirrezabala et al, 2015;DiMaio et al, 2015). Additionally, the structure of rod-shaped Barley stripe mosaic virus (BSMV, genus Hordeivirus) has recently been obtained at near-atomic resolution, showing striking differences from TMV in intersubunit contacts (Clare et al, 2015).…”

Section: Progress In Structural Studies Of Helical Virusesmentioning

confidence: 99%

“…The lateral inter-subunit contact is made by the CP Nterminal region, a part of which represents an 'interacting arm' (the IA domain) extending to a neighbouring subunit and interacting with a hydrophobic groove, or pocket, formed by the neighbouring subunit on the outer virion surface (Agirrezabala et al, 2015;DiMaio et al, 2015;Yang et al, 2012) (Protein Data Bank accession numbers 4DOX, 5A2T and 5FN1) (Fig. 2a, b).…”

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

confidence: 99%

“…In Bamboo mosaic virus (BaMV) virions, the IA domain forms a short a-helix located in the hydrophobic groove of the neighbouring subunit; additionally, Trp41 of one protein subunit forms a strong stacking interaction with Trp68 of another CP molecule (DiMaio et al, 2015). The IA domain of Pepino mosaic virus (PepMV) comprises Phe28, functionally analogous to PapMV Phe13 and BaMV Trp41 (Agirrezabala et al, 2015). The Phe28 residue is crucial for PapMV capsid assembly, since a point mutation affecting this residue results in a virus unable to form stable virions (Agirrezabala et al, 2015).…”

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

confidence: 99%

“…The IA domain of Pepino mosaic virus (PepMV) comprises Phe28, functionally analogous to PapMV Phe13 and BaMV Trp41 (Agirrezabala et al, 2015). The Phe28 residue is crucial for PapMV capsid assembly, since a point mutation affecting this residue results in a virus unable to form stable virions (Agirrezabala et al, 2015). Similarly, a deletion affecting the IA domain in PapMV CP, as well as a mutation in PapMV CP Phe13, completely abolishes homologous protein-protein interactions (Lecours et al, 2006).…”

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

confidence: 99%

“…The C-terminal region of potexvirus CP is involved in axial inter-subunit contacts (Agirrezabala et al, 2015;DiMaio et al, 2015). The C-terminus is located on the inner virion surface and represents a long coil making multiple relatively weak contacts.…”

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

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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Section: Progress In Structural Studies Of Helical Virusesmentioning

confidence: 99%

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

confidence: 99%

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

confidence: 99%

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

confidence: 99%

Section: Flexible Inter-subunit Contacts In Potexvirusesmentioning

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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Potexviruses and Carlaviruses – Short Filamentous Viruses

Rubino

2022

Encyclopedia of Life Sciences

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Potexviruses and carlaviruses are plant‐infecting viruses belonging to the family Aphaflexiviridae and Betaflexiviridae , respectively. Both have slightly flexuous filamentous particles measuring 470–580 × 13 nm (potexviruses), and 610–700 × 12–15 nm (carlaviruses). Virions contain 94–95% protein and 5–6% positive sense, single‐stranded ribonucleic acid c . 5800–7000 nucleotides (nt) (potexviruses) and 7900–9000 nt (carlaviruses) in size. Both virus types have a genome with a similar structural organisation, comprising five (potexviruses) or six (carlaviruses) open reading frames, three of which, known as the ‘triple gene block’, encode polypeptides that facilitate virus movement within the host. Natural hosts of both virus types are herbaceous (weeds, ornamentals, vegetables) rather than woody plants. Many potexviruses are agents of severe diseases, whereas a high percentage of carlaviruses induce symptomless infections. Transmission of potexviruses in nature is, by and large, by mechanical contact, whereas carlaviruses are transmitted primarily by aphids with a nonpersistent modality. Key Concepts Potexviruses and carlaviruses infect primarily herbaceous hosts after mechanical or vector‐driven transmission, respectively. Particles of both genera are filamentous and slightly flexuous and accumulate in aggregates in the cytoplasm of parenchyma cells. Demarcation of species within the genera takes into account molecular and biological criteria. Both genera are characterised by the presence of the so‐called triple gene block that provides the support for virus movement in infected hosts. Potexviruses and carlaviruses constitute models for virus replication, movement and encapsidation studies. Control is based on preventive measures, such as sanitary selection, production of virus‐free seed lots and resistance through conventional breeding and genetic engineering.

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Near atomic structure of flexible filamentous pepino mosaic virus by high resolution cryo‐ EM

Agirrezabala

Méndez

Sánchez-Pina

et al. 2016

European Microscopy Congress 2016: Proceedings

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Flexible filamentous viruses belonging to the Alphaflexiviridae family cause from severe to mild diseases in agricultural crops, often reducing yield and crop quality. Viral particles from the Alphaflexiviridae group are formed by a (+)ssRNA molecule encapsidated by single capsid protein (CP) monomers arranged in helical fashion. Pepino mosaic virus (PepMV) is a flexible filamentous plant virus belonging to the genus Potexvirus included in the family Alphaflexiviridae which genome consists of a ~6.4 kb (+)ssRNA and encodes five proteins. We report here the structure of intact PepMV virions by cryoEM at 3.9 Å resolution (Agirrezabala et al., 2015). The results and the resolution achieved (Figure 1) allowed the modeling of the CP, the (+)ssRNA and their relative interactions. The CP was modeled starting with the CP from PapMV (Yang et al., 2012), clearly showing a similar folding of the α‐helical domain for the Alphaflexiviridae family. The ssRNA is allocated and protected in a continuous groove of high electropositive potential built up by the CP in helical arrangement. The CP polymerize through a flexible N‐terminal arm providing the structural basis for the flexibility of the virus, in similar organization as the observed for BaMV (DiMaio et al., 2015). Interestingly, the overall structure and organization of CP from PepMV is similar to the organization of nucleoproteins from the Bunyaviridae family, a group of enveloped (‐)ssRNA viruses. Common features include: the folding and arrangement of the α‐helical main domain; the groove for the ssRNA; the N‐terminal arm for polymerization; and the relative position between all these elements. Although structural homology between viruses revealed by their atomic structures is common, in the current case, the different nature of capsid protein and nucleoprotein might have profound evolutionary implications.

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The near-atomic cryoEM structure of a flexible filamentous plant virus shows homology of its coat protein with nucleoproteins of animal viruses

Cited by 63 publications

References 33 publications

Helical capsids of plant viruses: architecture with structural lability

Helical capsids of plant viruses: architecture with structural lability

Potexviruses and Carlaviruses – Short Filamentous Viruses

Near atomic structure of flexible filamentous pepino mosaic virus by high resolution cryo‐ EM

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