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7OG6

Structure of Alternanthera Mosaic VLP by cryoEM

Summary for 7OG6
Entry DOI10.2210/pdb7og6/pdb
EMDB information12879
DescriptorCoat protein, RNA (5'-R(P*UP*UP*UP*UP*U)-3') (2 entities in total)
Functional Keywordspotexvirus, virus like particle, vlp.
Biological sourceAlternanthera mosaic virus
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Total number of polymer chains2
Total formula weight23729.77
Authors
Byrne, M.J.,Ranson, N.A.,Lomonossoff, G.P.,Thuenemann, E.C. (deposition date: 2021-05-06, release date: 2021-06-23, Last modification date: 2025-07-09)
Primary citationThuenemann, E.C.,Byrne, M.J.,Peyret, H.,Saunders, K.,Castells-Graells, R.,Ferriol, I.,Santoni, M.,Steele, J.F.C.,Ranson, N.A.,Avesani, L.,Lopez-Moya, J.J.,Lomonossoff, G.P.
A Replicating Viral Vector Greatly Enhances Accumulation of Helical Virus-Like Particles in Plants.
Viruses, 13:-, 2021
Cited by
PubMed Abstract: The production of plant helical virus-like particles (VLPs) via plant-based expression has been problematic with previous studies suggesting that an RNA scaffold may be necessary for their efficient production. To examine this, we compared the accumulation of VLPs from two potexviruses, papaya mosaic virus and alternanthera mosaic virus (AltMV), when the coat proteins were expressed from a replicating potato virus X- based vector (pEff) and a non-replicating vector (pEAQ-). Significantly greater quantities of VLPs could be purified when pEff was used. The pEff system was also very efficient at producing VLPs of helical viruses from different virus families. Examination of the RNA content of AltMV and tobacco mosaic virus VLPs produced from pEff revealed the presence of vector-derived RNA sequences, suggesting that the replicating RNA acts as a scaffold for VLP assembly. Cryo-EM analysis of the AltMV VLPs showed they had a structure very similar to that of authentic potexvirus particles. Thus, we conclude that vectors generating replicating forms of RNA, such as pEff, are very efficient for producing helical VLPs.
PubMed: 34064959
DOI: 10.3390/v13050885
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.3 Å)
Structure validation

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