VPg impact on Ryegrass mottle virus serine-like 3C protease proteolysis and structure

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). NMR studies show a Pro-VPg complex interaction and VPg tertiary s...

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Published in:bioRxiv
Main Authors: Kalnins, Gints, Ludviga, Rebeka, Kalnciema, Ieva, Resevica, Gunta, Zeltina, Vilija, Bogans, Janis, Tars, Kaspars, Zeltins, Andris, Balke, Ina
Format: Paper
Language:English
Published: Cold Spring Harbor Cold Spring Harbor Laboratory Press 20.01.2023
Cold Spring Harbor Laboratory
Edition:1.1
Subjects:
Crystal structure
Genomes
Microbiology
NMR
Nuclear magnetic resonance
Protein structure
Proteolysis
Serine
Tertiary structure
Viruses
Zinc
VPg
ryegrass mottle virus
serine-like 3C proteases
ISSN:2692-8205, 2692-8205
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Summary: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). NMR 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 ProVPg 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 activities on the Pro cleavage activity.Competing Interest StatementThe authors have declared no competing interest.
Bibliography:SourceType-Working Papers-1
ObjectType-Working Paper/Pre-Print-1
content type line 50
Competing Interest Statement: The authors have declared no competing interest.
ISSN:2692-8205
2692-8205
DOI:10.1101/2023.01.19.524839