Project description:In this work, we report the near-complete genome sequence of ryegrass mottle virus identified in irrigation water through next-generation sequencing and de novo assembly. The genome is 4,247 bp long, arranged in five open reading frames with a 5' untranslated region (UTR) of 87 nucleotides and a 3' UTR of 247 nucleotides.

| S-EPMC8103856 | biostudies-literature

VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure.

Project description:Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its cis and trans activity is mediated by the naturally unfolded virus-genome-linked protein (VPg). Nuclear magnetic resonance studies show a Pro-VPg complex interaction and VPg tertiary structure; however, information regarding structural changes of the Pro-VPg complex during interaction is lacking. Here, we solved a full Pro-VPg 3D structure of ryegrass mottle virus (RGMoV) that demonstrates the structural changes in three different conformations due to VPg interaction with Pro. We identified a unique site of VPg interaction with Pro that was not observed in other sobemoviruses, and observed different conformations of the Pro β2 barrel. This is the first report of a full plant Pro crystal structure with its VPg cofactor. We also confirmed the existence of an unusual previously unmapped cleavage site for sobemovirus Pro in the transmembrane domain: E/A. We demonstrated that RGMoV Pro in cis activity is not regulated by VPg and that in trans, VPg can also mediate Pro in free form. Additionally, we observed Ca2+ and Zn2+ inhibitory effects on the Pro cleavage activity.

| S-EPMC10048871 | biostudies-literature

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