VPg-mediated Aggregation of Potyviral RNA

Luciano, Carl S.; Murphy, John F.; Rhoads, Robert E.; Shaw, J. G.

doi:10.1099/0022-1317-72-1-205

Cited by 8 publications

(2 citation statements)

References 19 publications

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“…It seems thus that the VPg dimer arises during VPg purification or manipulation, when atmospheric oxygen induces formation of disulfide bonds. It is worth noting that the RNAs prepared from three different potyviruses were found in an apparently VPgdependent aggregated form (37). The propensity for oligomerization has been observed previously for VPg proteins of clover yellow vein virus (38) and turnip mosaic virus (14).…”

Section: Resultssupporting

confidence: 59%

Virulence Factor of Potato Virus Y, Genome-attached Terminal Protein VPg, Is a Highly Disordered Protein

Grzela

Szołajska

Ebel

et al. 2008

Journal of Biological Chemistry

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Potato virus Y (PVY) is a common potyvirus of agricultural importance, belonging to the picornavirus superfamily of RNA plus-stranded viruses. A covalently linked virus-encoded protein VPg required for virus infectivity is situated at the 5 end of potyvirus RNA. VPg seems to be involved in multiple interactions, both with other viral products and host proteins. VPgs of potyviruses have no known homologs, and there is no atomic structure available. To understand the molecular basis of VPg multifunctionality, we have analyzed structural features of VPg from PVY using structure prediction programs, functional assays, and biochemical and biophysical analyses. Structure predictions suggest that VPg exists in a natively unfolded conformation. In contrast with ordered proteins, PVY VPg is not denatured by elevated temperatures, has sedimentation values incompatible with a compact globular form, and shows a CD spectrum of a highly disordered protein, and HET-HETSOFAST NMR analysis suggests the presence of large unstructured regions. Although VPg has a propensity to form dimers, no functional differences were seen between the monomer and dimer. These data strongly suggest that the VPg of PVY should be classified among intrinsically disordered proteins. Intrinsic disorder lies at the basis of VPg multifunctionality, which is necessary for virus survival in the host.

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Section: Resultssupporting

confidence: 59%

Virulence Factor of Potato Virus Y, Genome-attached Terminal Protein VPg, Is a Highly Disordered Protein

Grzela

Szołajska

Ebel

et al. 2008

Journal of Biological Chemistry

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“…The VPg–VPg interaction reported here is a novel observation for PSbMV and is supported by the more extensive studies carried out on the self-interaction of PVA VPg (Oruetxebarria et al , 2001 ). The potyviral VPg protein mediates aggregation of viral RNA (Luciano et al , 1991 ) and the VPg–VPg interaction might facilitate recruitment of virus replication and/or translation complexes to the right position on the viral genomic RNA.…”

Section: Full Textmentioning

confidence: 99%

Towards a protein interaction map of potyviruses: protein interaction matrixes of two potyviruses based on the yeast two-hybrid system

Guo

Rajamäki

Saarma

et al. 2001

Journal of General Virology

118

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A map for the interactions of the major proteins from Potato virus A (PVA) and Pea seed-borne mosaic virus (PSbMV) (members of the genus Potyvirus, family Potyviridae) was generated using the yeast two-hybrid system (YTHS). Interactions were readily detected with five PVA protein combinations (HC-HC, HC-CI, VPg-VPg, NIa-NIb and CP-CP) and weak but reproducible interactions were detected for seven additional combinations (P1-CI, P3-NIb, NIaPro-NIb, VPg-NIa, VPg-NIaPro, NIaPro-NIa and NIa-NIa). In PSbMV, readily detectable interactions were found in five protein combinations (HC-HC, VPg-VPg, VPg-NIa, NIa-NIa and NIa-NIb) and weaker but reproducible interactions were detected for three additional combinations (P3-NIa, NIa-NIaPro and CP-CP). The self-interactions of HC, VPg, NIa and CP and the interactions of VPg-NIa, NIa-NIaPro and NIa-NIb were, therefore, common for the two potyviruses. The multiple protein interactions revealed in this study shed light on the co-ordinated functions of potyviral proteins involved in virus movement and replication.Interactions between proteins play pivotal roles in many processes during the virus infection cycle ; for example, in the formation of virus replication complexes, assembly of virions, virus movement between cells and virus transmission between plants by vectors. Analysis of protein-protein interactions is crucial for understanding protein functions and the molecular mechanisms underlying biological processes. The classical and more recent methods for detecting protein interactions have been reviewed previously

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Comparative sequence analysis and expression of bovine PrP gene in mouse L-929 cells

et al. 1992

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A cDNA clone encoding bovine scrapie-associated fibril protein, PrP, from a bovine brain cDNA library and six amplified genomic DNA clones of bovine PrP were characterized. These clones possessed specific characteristics observed in other animal PrP genes. However, the bovine PrP was divided into two types by the number of repeats. One possessed four octapeptide repetitive sequences, like other animal PrP genes, and consisted of 256 amino acids; the other had five such repetitive sequences and 264 amino acids. The amino acid sequence of the former bovine PrP agreed with that of sheep PrP up to the 165th amino acid from the N-terminus. Bovine PrP cDNA introduced into mouse L-929 cells were stably expressed. The expression level of recombinant bovine PrP in the cells judged by immunofluorescence was higher than that of authentic mouse PrP. The recombinant PrP comigrated with authentic bovine PrP in SDS-polyacrylamide gel electrophoresis, suggesting that the recombinant product was fully glycosylated in L-929 cells. Distinct bundles of the intermediate filaments were frequently seen at the perinuclear region of the cells.

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VPg-mediated Aggregation of Potyviral RNA

Cited by 8 publications

References 19 publications

Virulence Factor of Potato Virus Y, Genome-attached Terminal Protein VPg, Is a Highly Disordered Protein

Virulence Factor of Potato Virus Y, Genome-attached Terminal Protein VPg, Is a Highly Disordered Protein

Towards a protein interaction map of potyviruses: protein interaction matrixes of two potyviruses based on the yeast two-hybrid system

Comparative sequence analysis and expression of bovine PrP gene in mouse L-929 cells

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