6sco
From Proteopedia
Cryo-EM Structure of Potato Leaf Roll Virus VLP
Structural highlights
FunctionCAPSD_PLRV1 Major capsid protein that self-assembles to form an icosahedral capsid with a T=3 symmetry, about 23 nm in diameter, and consisting of 180 capsid proteins monomers (PubMed:31611039, PubMed:34813955). Most of the 180 monomers are the major capsid protein, but a small percentage contain the minor capsid protein, which has a long C-terminal extension (PubMed:31611039).[1] [2] Publication Abstract from PubMedThe Luteoviridae are pathogenic plant viruses responsible for significant crop losses worldwide. They infect a wide range of food crops, including cereals, legumes, cucurbits, sugar beet, sugarcane, and potato and, as such, are a major threat to global food security. Viral replication is strictly limited to the plant vasculature, and this phloem limitation, coupled with the need for aphid transmission of virus particles, has made it difficult to generate virus in the quantities needed for high-resolution structural studies. Here, we exploit recent advances in heterologous expression in plants to produce sufficient quantities of virus-like particles for structural studies. We have determined their structures to high resolution by cryoelectron microscopy, providing the molecular-level insight required to rationally interrogate luteovirid capsid formation and aphid transmission, thereby providing a platform for the development of preventive agrochemicals for this important family of plant viruses. Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles.,Byrne MJ, Steele JFC, Hesketh EL, Walden M, Thompson RF, Lomonossoff GP, Ranson NA Structure. 2019 Oct 8. pii: S0969-2126(19)30316-8. doi:, 10.1016/j.str.2019.09.010. PMID:31611039[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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