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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Vydáno v:	International journal of molecular sciences Ročník 24; číslo 6; s. 5347
Hlavní autoři:	Kalnins, Gints, Ludviga, Rebeka, Kalnciema, Ieva, Resevica, Gunta, Zeltina, Vilija, Bogans, Janis, Tars, Kaspars, Zeltins, Andris, Balke, Ina
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	Switzerland MDPI AG 10.03.2023 MDPI
Témata:	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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Abstract	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.
AbstractList	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. 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.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. 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 Ca[sup.2+] and Zn[sup.2+] inhibitory effects on the Pro cleavage activity. Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its and 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 activity is not regulated by VPg and that , VPg can also mediate Pro in free form. Additionally, we observed Ca and Zn inhibitory effects on the Pro cleavage activity.
Audience	Academic
Author	Zeltins, Andris Kalnciema, Ieva Bogans, Janis Tars, Kaspars Ludviga, Rebeka Resevica, Gunta Kalnins, Gints Zeltina, Vilija Balke, Ina
AuthorAffiliation	2 Plant Virus Protein Research Group, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia 4 Biotechnology Core Facility, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia 3 Plant Virology Group, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia 1 Structural Biology Group, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia
AuthorAffiliation_xml	– name: 1 Structural Biology Group, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia – name: 4 Biotechnology Core Facility, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia – name: 3 Plant Virology Group, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia – name: 2 Plant Virus Protein Research Group, Latvian Biomedical Research and Study Centre, Ratsupites Street 1, k-1, LV-1067 Riga, Latvia
Author_xml	– sequence: 1 givenname: Gints surname: Kalnins fullname: Kalnins, Gints – sequence: 2 givenname: Rebeka surname: Ludviga fullname: Ludviga, Rebeka – sequence: 3 givenname: Ieva surname: Kalnciema fullname: Kalnciema, Ieva – sequence: 4 givenname: Gunta surname: Resevica fullname: Resevica, Gunta – sequence: 5 givenname: Vilija surname: Zeltina fullname: Zeltina, Vilija – sequence: 6 givenname: Janis surname: Bogans fullname: Bogans, Janis – sequence: 7 givenname: Kaspars surname: Tars fullname: Tars, Kaspars – sequence: 8 givenname: Andris surname: Zeltins fullname: Zeltins, Andris – sequence: 9 givenname: Ina orcidid: 0000-0002-5171-7744 surname: Balke fullname: Balke, Ina
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Keywords	ryegrass mottle virus serine-like 3C proteases Sobemovirus VPg
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Snippet	Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its cis and trans... Sobemoviruses encode serine-like 3C proteases (Pro) that participate in the processing and maturation of other virus-encoded proteins. Its and activity is...
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SubjectTerms	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
Title	VPg Impact on Ryegrass Mottle Virus Serine-like 3C Protease Proteolysis and Structure
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