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Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles
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 li...
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Cell Press
2019
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6899511/ https://www.ncbi.nlm.nih.gov/pubmed/31611039 http://dx.doi.org/10.1016/j.str.2019.09.010 |
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author | Byrne, Matthew J. Steele, John F.C. Hesketh, Emma L. Walden, Miriam Thompson, Rebecca F. Lomonossoff, George P. Ranson, Neil A. |
author_facet | Byrne, Matthew J. Steele, John F.C. Hesketh, Emma L. Walden, Miriam Thompson, Rebecca F. Lomonossoff, George P. Ranson, Neil A. |
author_sort | Byrne, Matthew J. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-6899511 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2019 |
publisher | Cell Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-68995112020-01-21 Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles Byrne, Matthew J. Steele, John F.C. Hesketh, Emma L. Walden, Miriam Thompson, Rebecca F. Lomonossoff, George P. Ranson, Neil A. Structure Article 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. Cell Press 2019-12-03 /pmc/articles/PMC6899511/ /pubmed/31611039 http://dx.doi.org/10.1016/j.str.2019.09.010 Text en © 2019 The Authors http://creativecommons.org/licenses/by/4.0/ This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Byrne, Matthew J. Steele, John F.C. Hesketh, Emma L. Walden, Miriam Thompson, Rebecca F. Lomonossoff, George P. Ranson, Neil A. Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles |
title | Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles |
title_full | Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles |
title_fullStr | Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles |
title_full_unstemmed | Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles |
title_short | Combining Transient Expression and Cryo-EM to Obtain High-Resolution Structures of Luteovirid Particles |
title_sort | combining transient expression and cryo-em to obtain high-resolution structures of luteovirid particles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6899511/ https://www.ncbi.nlm.nih.gov/pubmed/31611039 http://dx.doi.org/10.1016/j.str.2019.09.010 |
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