Luteovirus group 1 coat protein / Luteovirus coat protein / T=3 icosahedral viral capsid / Viral coat protein subunit / viral capsid / structural molecule activity / Major capsid protein / Coat protein
Biotechnology and Biological Sciences Research Council
BB/R00160X/1
英国
Wellcome Trust
108466/Z/15/Z
英国
Biotechnology and Biological Sciences Research Council
BB/L014130/1
英国
Biotechnology and Biological Sciences Research Council
BB/J004596/1
英国
Biotechnology and Biological Sciences Research Council
BBS/E/000PR9794
英国
引用
ジャーナル: Structure / 年: 2019 タイトル: Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. 著者: Matthew J Byrne / John F C Steele / Emma L Hesketh / Miriam Walden / Rebecca F Thompson / George P Lomonossoff / Neil A Ranson / 要旨: The 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, ...The 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.