Science Advances

Supplementary Materials

The PDF file includes:

  • Supplementary Text S1. Detailed description of protein-protein interactions in PVY
  • Supplementary Text S2. Detailed description of protein-protein interactions in VLP
  • Supplementary Text S3. Importance of the CP N terminus for longitudinal assembly of VLPs
  • Supplementary Text S4. Redundancy of CP C termini for VLP filament or octameric ring
  • Fig. S1. Cryo-EM data collection, image processing, and model building for the PVY virion.
  • Fig. S2. Consensus sequence alignment of potyviral CPs.
  • Fig. S3. Biophysical characterization of PVY virions and various VLP constructs.
  • Fig. S4. Structural comparison of PVY to other filamentous viruses, flexible and rod shaped.
  • Fig. S5. Details of the PVY interaction network.
  • Fig. S6. Electrostatic interactions are crucial for PVY virion assembly.
  • Fig. S7. Cryo-EM data collection, image processing, and model building for VLP.
  • Fig. S8. Surface electrostatic potential of VLPs.
  • Fig. S9. Water channels in different types of filamentous particles.
  • Table S1. Cryo-EM data collection and refinement statistics of PVY and VLP.
  • Table S2. Primers and probes used for in planta functional analysis of PVY mutants and their properties.
  • Legend for data S1
  • Legend for tables S3 to S5
  • References (5660)

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Other Supplementary Material for this manuscript includes the following:

  • Data S1 (Microsoft Excel format). Relative concentration of PVY RNA as measured in the leaves of N. clevelandii including tables S3 to S5:
  • Table S3. Relative concentration of PVY RNA as measured in bombarded leaves of N. clevelandii 7 dpb (experiment 1).
  • Table S4. Relative concentration of PVY RNA as measured in upper nonbombarded leaves of N. clevelandii 14 dpb (experiment 1).
  • Table S5. Relative concentration of PVY RNA as measured in bombarded leaves of N. clevelandii (experiment 2).

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