The charged residues in the surface-exposed C-terminus of the Soybean mosaic virus coat protein are critical for cell-to-cell movement

Seo, Jang‐Kyun; Phan, Mi Sa Vo; Kang, Seong-Gil; Choi, Hyun-Sug; Kim, Kook‐Hyung

doi:10.1016/j.virol.2013.07.033

Cited by 37 publications

(26 citation statements)

References 33 publications

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“…We previously developed a useful viral vector system by engineering SMV-G7H to express foreign genes in soybean and by tagging the SMV vector with a GUS gene; using this system, we were able to visualize virus infection and movement in plant cells2728. The same strategy was used to tag SMV-G5H with GUS (Fig.…”

Section: Resultsmentioning

confidence: 99%

“…The resulting construct with the GmPP2C3a insert in the correct orientation was named pSMV-G7H-GmPP2C3a. The same strategy was used to construct SMV-G5H-based viral vector carrying the cloning sites ( Xba I and Mlu I) between P1 and HC-Pro as described previously28, and the amplified GUS gene was inserted into the XbaI site to generate pSMV-G5H-GUS as described previously27. For simultaneous expression of GUS and GmPP2C3a, an additional NIa-Pro cleavage site and the cloning sites ( Sal I and Sna BI) were engineered into the polyprotein ORF between the Nib and CP cistrons of pSMV-G7H-GUS as described previously47; the resulting construct was named pSMV-G7H-GUS-MCS.…”

Section: Methodsmentioning

confidence: 99%

“…GUS expression driven by virus infection was examined at 5 dpi by histochemical GUS assays as described previously27. Detection of callose deposition was performed at 5 dpi by the aniline blue staining method as described previously48.…”

Section: Methodsmentioning

confidence: 99%

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Type 2C Protein Phosphatase Is a Key Regulator of Antiviral Extreme Resistance Limiting Virus Spread

Seo

Kwon

Cho

et al. 2014

Sci Rep

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Effector-triggered immunity (ETI) is an active immune response triggered by interactions between host resistance proteins and their cognate effectors. Although ETI is often associated with the hypersensitive response (HR), various R genes mediate an HR-independent process known as extreme resistance (ER). In the soybean-Soybean mosaic virus (SMV) pathosystem, the strain-specific CI protein of SMV functions as an effector of Rsv3-mediated ER. In this study, we used the soybean (Rsv3)-SMV (CI) pathosystem to gain insight into the molecular signaling pathway involved in ER. We used genome-wide transcriptome analysis to identify a subset of the type 2C protein phophatase (PP2C) genes that are specifically up-regulated in Rsv3-mediated ER. Gain-of-function analysis of the most significantly expressed soybean PP2C gene, GmPP2C3a, showed that ABA-induced GmPP2C3a functions as a key regulator of Rsv3-mediated ER. Our results further suggest that the primary mechanism of ER against viruses is the inhibition of viral cell-to-cell movement by callose deposition in an ABA signaling-dependent manner.

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Section: Resultsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

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Type 2C Protein Phosphatase Is a Key Regulator of Antiviral Extreme Resistance Limiting Virus Spread

Seo

Kwon

Cho

et al. 2014

Sci Rep

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“…Mutations introduced into the core domain of the potyvirus Tobacco etch virus CP result in the inability of the protein to form virions and virus incompetence for cell-to cell-movement, whereas deletions in either the N-or C-terminal CP regions, which are dispensable for virion formation, do not abolish viral cell-to-cell movement, although they do make it slower compared with the wildtype virus (Dolja et al, 1994(Dolja et al, , 1995. In a similar manner, point mutations in the CP C-terminal region of Soybean mosaic virus, another potyvirus, block both virion formation and viral cell-to cell movement (Seo et al, 2013), indicating a direct link between them. Furthermore, immuno-gold labelling and electron microscopy studies have revealed the potyvirus CP in plasmodesmal cavities Rodríguez-Cerezo et al, 1997), and its localization within plasmodesmata often correlates with the presence of CPcontaining fibrillar material, with the dimensions of fibrils similar to the virion diameter .…”

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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“…Potyviral capsid proteins (CPs) not only form the viral particle but also participate in cell-to-cell and systemic movement (6,7). The variable N-and C-terminal regions of the CPs exposed on the virion surface are required for long-distance transport, are involved in aphid transmission (DAG motif), and may also assist in cell-to-cell spreading (7)(8)(9)(10), whereas the conserved core regions of CPs are necessary for virion assembly and the cell-to-cell movement of potyviruses (6,7).…”

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confidence: 99%

A Strategy for Generating a Broad-Spectrum Monoclonal Antibody and Soluble Single-Chain Variable Fragments against Plant Potyviruses

Liu

Lin

et al. 2015

Appl Environ Microbiol

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Potyviruses are major pathogens that often cause mixed infection in calla lilies. To reduce the time and cost of virus indexing, a detection method for the simultaneous targeting of multiple potyviruses was developed by generating a broad-spectrum monoclonal antibody (MAb) for detecting the greatest possible number of potyviruses. The conserved 121-amino-acid core regions of the capsid proteins of Dasheen mosaic potyvirus (DsMV), Konjak mosaic potyvirus (KoMV), and Zantedeschia mild mosaic potyvirus (ZaMMV) were sequentially concatenated and expressed as a recombinant protein for immunization. After hybridoma cell fusion and selection, one stable cell line that secreted a group-specific antibody, named C4 MAb, was selected. In the reaction spectrum test, the C4 MAb detected at least 14 potyviruses by indirect enzyme-linked immunosorbent assay (I-ELISA) and Western blot analysis. Furthermore, the variable regions of the heavy (V H ) and light (V L ) chains of the C4 MAb were separately cloned and constructed as single-chain variable fragments (scFvs) for expression in Escherichia coli. Moreover, the pectate lyase E (PelE) signal peptide of Erwinia chrysanthemi S3-1 was added to promote the secretion of C4 scFvs into the medium. According to Western blot analysis and I-ELISA, the soluble C4 scFv (V L -V H ) fragment showed a binding specificity similar to that of the C4 MAb. Our results demonstrate that a recombinant protein derived from fusion of the conserved regions of viral proteins has the potential to produce a broad-spectrum MAb against a large group of viruses and that the PelE signal peptide can improve the secretion of scFvs in E. coli. The genus Potyvirus, one of the largest groups of plant viruses, includes 158 species, many of which are economically important, such as Potato virus Y (PVY) and Plum pox virus (1, 2). Most potyviruses infect various host plants and are spread worldwide by aphid vectors and mechanical inoculation (3). Potyviruses have a single-stranded, positive-sense RNA genome of approximately 10 kb in length that encodes a polyprotein translated from a large open reading frame (ORF) (3) and a trans-frame movement-related protein (P3N-PIPO) encoded from the 5=-terminal portion of P3 and the PIPO cistrons (4, 5). During proteolytic processing, the large polyprotein can be separated into 10 mature proteins that are involved in virus replication, movement, and virion assembly (3). Potyviral capsid proteins (CPs) not only form the viral particle but also participate in cell-to-cell and systemic movement (6, 7). The variable N-and C-terminal regions of the CPs exposed on the virion surface are required for long-distance transport, are involved in aphid transmission (DAG motif), and may also assist in cell-to-cell spreading (7-10), whereas the conserved core regions of CPs are necessary for virion assembly and the cell-to-cell movement of potyviruses (6, 7).In Taiwan, the viral disease caused by potyviruses is one of the limiting factors for production of calla lilies. At least five potyvirus...

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The charged residues in the surface-exposed C-terminus of the Soybean mosaic virus coat protein are critical for cell-to-cell movement

Cited by 37 publications

References 33 publications

Type 2C Protein Phosphatase Is a Key Regulator of Antiviral Extreme Resistance Limiting Virus Spread

Type 2C Protein Phosphatase Is a Key Regulator of Antiviral Extreme Resistance Limiting Virus Spread

Helical capsids of plant viruses: architecture with structural lability

A Strategy for Generating a Broad-Spectrum Monoclonal Antibody and Soluble Single-Chain Variable Fragments against Plant Potyviruses

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