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TitleSpecies-specific structural adaptation of the potyviral coat protein in virions and virus-like particles.
Journal, issue, pagesCommun Biol, Year 2026
Publish dateJan 13, 2026
AuthorsNeža Koritnik / Andreja Kežar / Luka Kavčič / Magda Tušek Žnidarič / Adrijana Leonardi / Swarnalok De / Maija Pollari / Kristiina Mäkinen / Marjetka Podobnik /
PubMed AbstractPotyviruses are the largest group of plant positive-sense single-stranded RNA viruses and represent a major economic burden worldwide. Their coat protein (CP) forms a filamentous, flexible capsid ...Potyviruses are the largest group of plant positive-sense single-stranded RNA viruses and represent a major economic burden worldwide. Their coat protein (CP) forms a filamentous, flexible capsid around the genomic RNA. However, information is still lacking on the mechanisms of virion assembly, disassembly and stability, which is central to understanding virus biology and control. Here, we investigate the role of CP in these processes using structural, biochemical and biophysical studies of five potyviral CPs from three phylogenetic clades combined with bioinformatics and in planta experiments. Our results suggest that, while potyviruses have a conserved virion structure, the amino acids forming the CP-CP and CP-RNA interactions leading to this structure are species-specific. We show that the species-specific CP sequence also determines the architecture of RNA-free virus-like particles (VLPs) and the degree of their structural polymorphism. We identify the residues that determine this specificity at distinct S1-S4 interaction sites. In contrast, a highly conserved charged amino acid triad at the CP-CP interface is essential for the stability of virions and RNA-free VLPs. These results contribute to understanding the molecular mechanism of potyviral virion assembly and highlight the significance of the amino acid sequence of selected CPs in potential biotechnological or biomedical applications.
External linksCommun Biol / PubMed:41530503
MethodsEM (helical sym.)
Resolution2.33 - 6.84 Å
Structure data

EMDB-53632: ssRNA-containing helical virus-like particle composed of PVA coat protein with 5 mutations (H89Q, E90S, S144E, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.49 Å

EMDB-53633: RNA-free helical (h8.7) virus-like particle composed of PVA coat protein with 5 mutations (H89Q, E90S, S144E, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.83 Å

EMDB-53634: RNA-free helical (h9.7) virus-like particle composed of PVA coat protein with 5 mutations (H89Q, E90S, S144E, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.84 Å

EMDB-53635: RNA-free stacked-ring (r10) virus-like particle composed of PVA coat protein with 5 mutations (H89Q, E90S, S144E, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.86 Å

EMDB-53636: RNA-free helical (h8.5) virus-like particle composed of PVA coat protein with R163A mutation
Method: EM (helical sym.) / Resolution: 3.36 Å

EMDB-53638: ssRNA-containing helical virus-like particle composed of PVY coat protein with Q87H mutation
Method: EM (helical sym.) / Resolution: 2.82 Å

EMDB-53639: RNA-free helical (h8.5) virus-like particle composed of PVY coat protein with Q87H mutation
Method: EM (helical sym.) / Resolution: 4.03 Å

EMDB-53640: RNA-free stacked-ring (r8) virus-like particle composed of PVY coat protein with Q87H mutation
Method: EM (helical sym.) / Resolution: 4.88 Å

EMDB-53642: ssRNA-containing helical virus-like particle composed of PVY coat protein with R208T mutation
Method: EM (helical sym.) / Resolution: 3.22 Å

EMDB-53643: RNA-free helical (h7.5) virus-like particle composed of PVY coat protein with R208T mutation
Method: EM (helical sym.) / Resolution: 6.84 Å

EMDB-53644: RNA-free helical (h8.5) virus-like particle composed of PVY coat protein with R208T mutation
Method: EM (helical sym.) / Resolution: 4.7 Å

EMDB-53645: RNA-free stacked-ring (r8) virus-like particle composed of PVY coat protein with R208T mutation
Method: EM (helical sym.) / Resolution: 3.86 Å

EMDB-53646: ssRNA-containing helical virus-like particle composed of PVY coat protein with Q87H and R208T mutations
Method: EM (helical sym.) / Resolution: 2.51 Å

EMDB-53647: RNA-free helical (h8.5) virus-like particle composed of PVY coat protein with Q87H and R208T mutations
Method: EM (helical sym.) / Resolution: 4.0 Å

EMDB-53650: ssRNA-containing helical virus-like particle composed of PVY coat protein with A161R mutation
Method: EM (helical sym.) / Resolution: 2.91 Å

EMDB-53651: RNA-free helical (h8.5) virus-like particle composed of PVA coat protein (in vitro assembly)
Method: EM (helical sym.) / Resolution: 3.63 Å

EMDB-53790, PDB-9r7r:
Potato virus A (PVA)
Method: EM (helical sym.) / Resolution: 2.39 Å

EMDB-53791, PDB-9r7s:
Potato virus A (PVA) after incubation in solution at 4C for 6 months
Method: EM (helical sym.) / Resolution: 2.54 Å

EMDB-53792, PDB-9r7t:
ssRNA-containing helical virus-like particle composed of PVA (isolate B11) coat protein
Method: EM (helical sym.) / Resolution: 2.54 Å

EMDB-53793, PDB-9r7u:
RNA-free helical (h8.5) virus-like particle composed of PVA (isolate B11) coat protein
Method: EM (helical sym.) / Resolution: 3.31 Å

EMDB-53794, PDB-9r7v:
ssRNA-containing helical virus-like particle composed of PVA (isolate Datura) coat protein
Method: EM (helical sym.) / Resolution: 3.06 Å

EMDB-53796, PDB-9r7x:
RNA-free helical (h8.5) virus-like particle composed of PVA (isolate Datura) coat protein
Method: EM (helical sym.) / Resolution: 2.63 Å

EMDB-53799, PDB-9r7y:
RNA-free helical (h9.7) virus-like particle composed of PVA coat protein with 6 mutations (H89Q, E90S, S144E, R163A, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.89 Å

EMDB-53800, PDB-9r7z:
RNA-free helical (h10.7) virus-like particle composed of PVA coat protein with 6 mutations (H89Q, E90S, S144E, R163A, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.92 Å

EMDB-53801, PDB-9r80:
RNA-free stacked-ring (r10) virus-like particle composed of PVA coat protein with 6 mutations (H89Q, E90S, S144E, R163A, K180E, and T210R)
Method: EM (helical sym.) / Resolution: 3.7 Å

EMDB-53802, PDB-9r81:
ssRNA-containing helical virus-like particle composed of PVA coat protein with D138C mutation
Method: EM (helical sym.) / Resolution: 2.33 Å

EMDB-53862, PDB-9r9w:
RNA-free helical (h8.5) virus-like particle composed of TEV coat protein
Method: EM (helical sym.) / Resolution: 3.34 Å

EMDB-53863, PDB-9r9x:
ssRNA-containing helical virus-like particle composed of PepMoV coat protein
Method: EM (helical sym.) / Resolution: 3.64 Å

EMDB-53864, PDB-9r9y:
RNA-free stacked-ring (r9) virus-like particle composed of PepMoV coat protein
Method: EM (helical sym.) / Resolution: 4.32 Å

EMDB-53865, PDB-9r9z:
ssRNA-containing helical virus-like particle composed of JGMV coat protein
Method: EM (helical sym.) / Resolution: 3.4 Å

EMDB-53866, PDB-9ra0:
RNA-free helical (h8.6) virus-like particle composed of JGMV coat protein
Method: EM (helical sym.) / Resolution: 4.44 Å

EMDB-53867, PDB-9ra1:
RNA-free helical (h9.6) virus-like particle composed of JGMV coat protein
Method: EM (helical sym.) / Resolution: 4.02 Å

EMDB-53868, PDB-9ra2:
RNA-free stacked-ring (r9) virus-like particle composed of JGMV coat protein
Method: EM (helical sym.) / Resolution: 3.51 Å

Source
  • potato virus a
  • Potato virus Y strain NTN
  • tobacco etch virus
  • pepper mottle virus
  • johnsongrass mosaic virus
KeywordsVIRUS / potato virus A / potyvirus / coat protein / RNA / helical / VIRUS LIKE PARTICLE / virus-like particle / tobacco etch virus / pepper mottle virus / Johnsongrass mosaic virus

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