AI Article Synopsis
- Luteoviruses, poleroviruses, and enamoviruses are insect-borne pathogens affecting various plants, including major food crops.
- Recent cryo-electron microscopy studies revealed that luteovirid viral capsids have a T = 3 icosahedral structure formed by a specific coat protein.
- The crystal structure of a truncated coat protein from the potato leafroll virus was determined at high resolution, highlighting its role in maintaining capsid symmetry and suggesting that the N-terminus of the coat protein is crucial for viral assembly and curvature.
Article Abstract
Luteoviruses, poleroviruses, and enamoviruses are insect-transmitted, agricultural pathogens that infect a wide array of plants, including staple food crops. Previous cryo-electron microscopy studies of virus-like particles show that luteovirid viral capsids are built from a structural coat protein that organizes with T = 3 icosahedral symmetry. Here, we present the crystal structure of a truncated version of the coat protein monomer from potato leafroll virus at 1.80-Å resolution. In the crystal lattice, monomers pack into flat sheets that preserve the two-fold and three-fold axes of icosahedral symmetry and show minimal structural deviations when compared to the full-length subunits of the assembled virus-like particle. These observations have important implications in viral assembly and maturation and suggest that the CP N-terminus and its interactions with RNA play an important role in generating capsid curvature.
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| http://dx.doi.org/10.1016/j.jsb.2021.107811 | DOI Listing |
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