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). Nuclear magnetic resonance studies show a Pro–VPg complex interac...

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Veröffentlicht in:International journal of molecular sciences Jg. 24; H. 6; S. 5347
Hauptverfasser: Kalnins, Gints, Ludviga, Rebeka, Kalnciema, Ieva, Resevica, Gunta, Zeltina, Vilija, Bogans, Janis, Tars, Kaspars, Zeltins, Andris, Balke, Ina
Format: Journal Article
Sprache:Englisch
Veröffentlicht: Switzerland MDPI AG 10.03.2023
MDPI
Schlagworte:
3C Viral Proteases
Amino Acid Sequence
Endopeptidases - metabolism
Enzymes
Genomes
Genomics
Gram-positive bacteria
Lolium - metabolism
NMR
Nuclear magnetic resonance
Peptide Hydrolases - metabolism
Peptides
Proteins
Proteolysis
RNA polymerase
RNA Viruses - metabolism
Scientific equipment and supplies industry
Serine
Serine - metabolism
Viral Proteins - metabolism
Viruses
Latvia
United States
Massachusetts
Germany
ryegrass mottle virus
serine-like 3C proteases
Sobemovirus
VPg
ISSN:1422-0067, 1661-6596, 1422-0067
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Zusammenfassung: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.
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These authors contributed equally to this work.
ISSN:1422-0067
1661-6596
1422-0067
DOI:10.3390/ijms24065347