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Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles.
Structure 2019S

Abstract

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.

Authors+Show Affiliations

Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK.Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK.Department of Biological Chemistry, John Innes Centre, Norwich Research Park, Colney, Norwich NR4 7UH, UK. Electronic address: george.lomonossoff@jic.ac.uk.Astbury Centre for Structural Molecular Biology, School of Molecular & Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds LS2 9JT, UK. Electronic address: n.a.ranson@leeds.ac.uk.

Pub Type(s)

Journal Article

Language

eng

PubMed ID

31611039

Citation

Byrne, Matthew J., et al. "Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles." Structure (London, England : 1993), 2019.
Byrne MJ, Steele JFC, Hesketh EL, et al. Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. Structure. 2019.
Byrne, M. J., Steele, J. F. C., Hesketh, E. L., Walden, M., Thompson, R. F., Lomonossoff, G. P., & Ranson, N. A. (2019). Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. Structure (London, England : 1993), doi:10.1016/j.str.2019.09.010.
Byrne MJ, et al. Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. Structure. 2019 Oct 8; PubMed PMID: 31611039.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles. AU - Byrne,Matthew J, AU - Steele,John F C, AU - Hesketh,Emma L, AU - Walden,Miriam, AU - Thompson,Rebecca F, AU - Lomonossoff,George P, AU - Ranson,Neil A, Y1 - 2019/10/08/ PY - 2019/04/04/received PY - 2019/06/17/revised PY - 2019/09/20/accepted PY - 2019/10/16/entrez KW - cryo-EM KW - homology modeling KW - luteovirus KW - plant virus KW - structure KW - virus JF - Structure (London, England : 1993) JO - Structure N2 - 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. SN - 1878-4186 UR - https://www.unboundmedicine.com/medline/citation/31611039/Combining_Transient_Expression_and_Cryo-EM_to_Obtain_High-Resolution_Structures_of_Luteovirid_Particles L2 - https://linkinghub.elsevier.com/retrieve/pii/S0969-2126(19)30316-8 DB - PRIME DP - Unbound Medicine ER -