7og6
From Proteopedia
Structure of Alternanthera Mosaic VLP by cryoEM
Structural highlights
FunctionQ52Z61_9VIRU Required for genome encapsidation. Forms ribonucleoprotein complexes along with TGB1 helicase and viral RNA.[ARBA:ARBA00004032] Publication Abstract from PubMedThe 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-HT). 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. A Replicating Viral Vector Greatly Enhances Accumulation of Helical Virus-Like Particles in Plants.,Thuenemann EC, Byrne MJ, Peyret H, Saunders K, Castells-Graells R, Ferriol I, Santoni M, Steele JFC, Ranson NA, Avesani L, Lopez-Moya JJ, Lomonossoff GP Viruses. 2021 May 11;13(5):885. doi: 10.3390/v13050885. PMID:34064959[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
|