The immobilized movement proteins of two tobamoviruses form stable ribonucleoprotein complexes with full‐length viral genomic RNA

Ivanov, Kostja I.; Иванов, П.А.; Timofeeva, E.K.; Dorokhov, Yuri L.; Atabekov, J.G.

doi:10.1016/0014-5793(94)00477-3

Cited by 19 publications

(1 citation statement)

References 20 publications

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“…Recombinant constructs expressing fusion (His) 6 proteins were generated by cloning the PCR-amplified fragments into the pQE plasmid vector (Qiagen). Restriction fragments were ligated into the corresponding sites of the expression vector as described by Ivanov et al (1994). All other methods used were in accordance with Sambrook et al (1989).…”

Section: Methodsmentioning

confidence: 99%

Immunogenic compositions assembled from tobacco mosaic virus-generated spherical particle platforms and foreign antigens

Карпова

Nikitin

Chirkov

et al. 2012

Journal of General Virology

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We reported recently that RNA-free spherical particles (SPs) generated by thermal remodelling of tobacco mosaic virus (TMV) are capable of binding GFP to their surface. Here, we show that SPs represent a universal particle platform that can form compositions by binding a diversity of various foreign proteins/epitopes of viral and non-viral origin to their surface. Numerous molecules of a foreign protein linked to the SP surface were revealed by immunogold electron microscopy. Several SP-based compositions were obtained containing one of the following foreign antigens: antigenic determinant A of rubella virus E1 glycoprotein; a recombinant protein containing the M2e epitope of influenza virus A protein M2; a recombinant antigen consisting of three epitopes of influenza virus A haemagglutinin; potato virus X (PVX) coat protein (CP); BSA; and PVX CP fused with the epitope of plum pox virus CP. The 'mixed' compositions could be also assembled by binding two different foreign antigens to each of the SPs. Immunogenicity of foreign antigens adsorbed or linked covalently to SPs in the SP-based compositions was examined. The antigenic specificity of foreign antigens was retained, whereas their immunogenicity increased significantly. It was inferred that SPs exhibit immunopotentiating activity, in particular in the form of compositions comprising SP and foreign antigen linked covalently to their surface by formaldehyde.

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Section: Methodsmentioning

confidence: 99%

Immunogenic compositions assembled from tobacco mosaic virus-generated spherical particle platforms and foreign antigens

Карпова

Nikitin

Chirkov

et al. 2012

Journal of General Virology

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Nontranslatability and Dissimilar Behavior in Plants and Protoplasts of Viral RNA and Movement Protein Complexes Formedin Vitro

et al. 1997

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It was found that the fusion (His)6-movement proteins (MPs) of two tobamoviruses (TMV UI and a crucifer-infecting tobamovirus, crTMV) were efficient nonspecific translational repressors. The in vitro translation of viral RNAs was blocked by incomplete 30K MP-RNA complexes formed at the MP:RNA molar ratios of 100-150:1. Similar results were obtained with the barley stripe mosaic hordeivirus (BSMV)-encoded 58K MP; however, the translation inhibiting activity of the 58K MP was manifested only in the presence of magnesium. By contrast, the 25K MP of potato virus X (PVX) was incapable of forming MP-RNA complexes under experimental conditions used and did not inhibit in vitro translation. The translation repressing ability correlated with the level of MP affinity to RNA. The complexes of the 30K MP and 58K MP with TMV RNA were not infectious in isolated protoplasts; however, they were infectious in indicator plants. Reduction of MP affinity to RNA resulted in translatability of MP-TMV RNA complexes that apparently was due to their destabilization. Thus, the deletion mutant DEL4 MP formed MP-TMV RNA complexes that were translatable in vitro, infectious to protoplasts and plants. In contrast to this, the complexes of TMV RNA with the mammalian RNA-binding protein p50 were nontranslatable and noninfectious to either protoplasts or intact plants. These results implied that nontranslatable MP-RNA complexes which could not replicate in the primary infected cells were converted into a translatable and replicatable form in the course of passage through plasmodesmata in planta.

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Phosphorylation of Tobacco Mosaic Virus Movement Protein Abolishes Its Translation Repressing Ability

et al. 1999

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Previously we showed that the ribonucleoprotein complexes (RNPs) of the TMV 30-kDa movement protein (MP) with TMV RNA are nontranslatable in vitro and noninfectious to protoplasts, but are infectious to intact plants. It has been suggested that MP-TMV RNA complexes could be converted into the translatable and replicatable form in planta in the course of passage through plasmodesmata (Karpova et al., 1997, Virology 230, 11-21). The role of TMV MP phosphorylation was investigated in terms of its capacity to modulate the translation-repressing ability of the MP. Phosphorylation of the TMV MP, either before or after RNP complex formation, caused a conversion of nontranslatable MP-RNA complexes into a form that was translatable in vitro and infectious to protoplasts and plants.

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The immobilized movement proteins of two tobamoviruses form stable ribonucleoprotein complexes with full‐length viral genomic RNA

Cited by 19 publications

References 20 publications

Immunogenic compositions assembled from tobacco mosaic virus-generated spherical particle platforms and foreign antigens

Immunogenic compositions assembled from tobacco mosaic virus-generated spherical particle platforms and foreign antigens

Nontranslatability and Dissimilar Behavior in Plants and Protoplasts of Viral RNA and Movement Protein Complexes Formedin Vitro

Phosphorylation of Tobacco Mosaic Virus Movement Protein Abolishes Its Translation Repressing Ability

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