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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. Copyright © 2021 Elsevier Inc. All rights reserved.


Myfanwy C Adams, Carl J Schiltz, Michelle L Heck, Joshua S Chappie. Crystal structure of the potato leafroll virus coat protein and implications for viral assembly. Journal of structural biology. 2022 Mar;214(1):107811

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PMID: 34813955

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