Structure of products of protein reassembly and reconstruction of potato virus X

Kaftanova, A.S.; Киселев, Н.А.; Novikov, V. K.; Atabekov, J.G.

doi:10.1016/0042-6822(75)90426-2

Cited by 18 publications

(16 citation statements)

References 16 publications

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“…However, partial aggregation of the PVX CP was rendered possible by adding phosphate buffer to the dialysed protein to a final concentration of 0.2 m (pH 7.0–7.5) and storing for 24 h at 4–20 °C. Thereafter, formation of single‐ and double‐layered protein discs could be revealed by electron microscopy (Kaftanova et al ., 1975). The diameter of discs was similar to that of the intact PVX particles.…”

Section: Repolimerization Of Pvx Cp In Vitromentioning

confidence: 99%

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Potato virus X: structure, disassembly and reconstitution

Atabekov

Dobrov

Карпова³

et al. 2007

Molecular Plant Pathology

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SUMMARY This paper summarizes some structural characteristics of Potato virus X (PVX), the flexuous filamentous plant potexvirus. A model of PVX coat protein (CP) tertiary structure in the virion proposed on the basis of tritium planigraphy combined with predictions of the protein tertiary structure is described. A possible role of glycosylation and phosphorylation in the CP structure and function is discussed. Two forms of PVX virion disassembly are discussed: (i) the virion co-translational disassembly after PVX CP in situ phosphorylation and (ii) disassembly of PVX triggered by different factors after linear destabilization of the virion by binding of the PVX-coded movement protein (TGBp1) to one end of the polar CP-helix. Special emphasis was placed on a translational activation of encapsidated PVX RNA and rapid disassembly of TGBp1-PVX complexes into free RNA and CP. The results of experiments on the PVX CP repolymerization and PVX reconstitution are considered. In particular, the products assembled from PVX RNA, CP and TGBp1 were examined. Single-tailed particles were found with a helical, head-like structure consisting of helically arranged CP subunits located at the 5'-tail of RNA; the TGBp1 was bound to the end of the head. Translatable 'RNA-CP-TGBp1' complexes may represent the transport form of the PVX infection.

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Section: Repolimerization Of Pvx Cp In Vitromentioning

confidence: 99%

“…Magnification, ×200 000. (c) Optical diffraction pattern of an electron micrograph of a disc stack (Kaftanova et al ., 1975).…”

Section: Repolimerization Of Pvx Cp In Vitromentioning

confidence: 99%

Potato virus X: structure, disassembly and reconstitution

Atabekov

Dobrov

Карпова³

et al. 2007

Molecular Plant Pathology

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“…13 Hence, the possibility of in situ PVX RNA degradation by RNases was examined. By contrast to TMV, encapsidated virion PVX RNA appeared sensitive to RNase treatment: no full-length RNA could be isolated from PVX particles treated with a mixture of RNase A and T1 ( Figure 5(a), lane 4).…”

Section: Rnase-treated Pvx Rna-deg Particles Containing Degraded Rnamentioning

confidence: 99%

Linear Remodeling of Helical Virus by Movement Protein Binding

Родионова

Карпова

Kozlovsky

et al. 2003

Journal of Molecular Biology

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“…The PVX CP is known not to form virus-like aggregates in the absence of RNA [16]. Particles that are morphologically indistinguishable from those obtained upon the reconstruction of PVX CP with homologous PVX RNA ( Fig.…”

Section: Resultsmentioning

confidence: 99%

Characteristics of Artificial Virus-like Particles Assembled in vitro from Potato Virus X Coat Protein and Foreign Viral RNAs

et al. 2011

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Potato virus X (PVX) and some other potexviruses can be reconstitutedin vitrofrom viral coat protein (CP) and RNA. PVX CP is capable of forming viral ribonucleoprotein complexes (vRNP) not only with homologous, but also with foreign RNAs. This paper presents the structure and properties of vRNP assembledin vitroupon incubation of PVX CP and RNAs of various plant and animal viruses belonging to different taxonomic groups. We have shown that the morphology and translational properties of vRNPs containing foreign (heterologous) RNA are identical to those of homological vRNP (PVX RNA – PVX CP). Our data suggest that the assembly of the “mixed” vRNPin vitrocould be started at the 5’-proximal region of the RNA, producing a helical structure of vRNPs with foreign nucleic acids. The formation of heterologous vRNPin vitrowith PVX CP appears not to require a specific 5’ end RNA nucleotide sequence, and the PVX CP seems to be able to pack foreign genetic material of various sizes and compositions into artificial virus-like particles.

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Structure of products of protein reassembly and reconstruction of potato virus X

Cited by 18 publications

References 16 publications

Potato virus X: structure, disassembly and reconstitution

Potato virus X: structure, disassembly and reconstitution

Linear Remodeling of Helical Virus by Movement Protein Binding

Characteristics of Artificial Virus-like Particles Assembled in vitro from Potato Virus X Coat Protein and Foreign Viral RNAs

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