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Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions
Understanding the structural diversity of honeybee-infecting viruses is critical to maintain pollinator health and manage the spread of diseases in ecology and agriculture. We determine cryo-EM structures of T = 4 and T = 3 capsids of virus-like particles (VLPs) of Lake Sinai virus (LSV) 2 and delta...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9892032/ https://www.ncbi.nlm.nih.gov/pubmed/36726015 http://dx.doi.org/10.1038/s41467-023-36235-3 |
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author | Chen, Nai-Chi Wang, Chun-Hsiung Yoshimura, Masato Yeh, Yi-Qi Guan, Hong-Hsiang Chuankhayan, Phimonphan Lin, Chien-Chih Lin, Pei-Ju Huang, Yen-Chieh Wakatsuki, Soichi Ho, Meng-Chiao Chen, Chun-Jung |
author_facet | Chen, Nai-Chi Wang, Chun-Hsiung Yoshimura, Masato Yeh, Yi-Qi Guan, Hong-Hsiang Chuankhayan, Phimonphan Lin, Chien-Chih Lin, Pei-Ju Huang, Yen-Chieh Wakatsuki, Soichi Ho, Meng-Chiao Chen, Chun-Jung |
author_sort | Chen, Nai-Chi |
collection | PubMed |
description | Understanding the structural diversity of honeybee-infecting viruses is critical to maintain pollinator health and manage the spread of diseases in ecology and agriculture. We determine cryo-EM structures of T = 4 and T = 3 capsids of virus-like particles (VLPs) of Lake Sinai virus (LSV) 2 and delta-N48 LSV1, belonging to tetraviruses, at resolutions of 2.3–2.6 Å in various pH environments. Structural analysis shows that the LSV2 capsid protein (CP) structural features, particularly the protruding domain and C-arm, differ from those of other tetraviruses. The anchor loop on the central β-barrel domain interacts with the neighboring subunit to stabilize homo-trimeric capsomeres during assembly. Delta-N48 LSV1 CP interacts with ssRNA via the rigid helix α1’, α1’–α1 loop, β-barrel domain, and C-arm. Cryo-EM reconstructions, combined with X-ray crystallographic and small-angle scattering analyses, indicate that pH affects capsid conformations by regulating reversible dynamic particle motions and sizes of LSV2 VLPs. C-arms exist in all LSV2 and delta-N48 LSV1 VLPs across varied pH conditions, indicating that autoproteolysis cleavage is not required for LSV maturation. The observed linear domino-scaffold structures of various lengths, made up of trapezoid-shape capsomeres, provide a basis for icosahedral T = 4 and T = 3 architecture assemblies. These findings advance understanding of honeybee-infecting viruses that can cause Colony Collapse Disorder. |
format | Online Article Text |
id | pubmed-9892032 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-98920322023-02-03 Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions Chen, Nai-Chi Wang, Chun-Hsiung Yoshimura, Masato Yeh, Yi-Qi Guan, Hong-Hsiang Chuankhayan, Phimonphan Lin, Chien-Chih Lin, Pei-Ju Huang, Yen-Chieh Wakatsuki, Soichi Ho, Meng-Chiao Chen, Chun-Jung Nat Commun Article Understanding the structural diversity of honeybee-infecting viruses is critical to maintain pollinator health and manage the spread of diseases in ecology and agriculture. We determine cryo-EM structures of T = 4 and T = 3 capsids of virus-like particles (VLPs) of Lake Sinai virus (LSV) 2 and delta-N48 LSV1, belonging to tetraviruses, at resolutions of 2.3–2.6 Å in various pH environments. Structural analysis shows that the LSV2 capsid protein (CP) structural features, particularly the protruding domain and C-arm, differ from those of other tetraviruses. The anchor loop on the central β-barrel domain interacts with the neighboring subunit to stabilize homo-trimeric capsomeres during assembly. Delta-N48 LSV1 CP interacts with ssRNA via the rigid helix α1’, α1’–α1 loop, β-barrel domain, and C-arm. Cryo-EM reconstructions, combined with X-ray crystallographic and small-angle scattering analyses, indicate that pH affects capsid conformations by regulating reversible dynamic particle motions and sizes of LSV2 VLPs. C-arms exist in all LSV2 and delta-N48 LSV1 VLPs across varied pH conditions, indicating that autoproteolysis cleavage is not required for LSV maturation. The observed linear domino-scaffold structures of various lengths, made up of trapezoid-shape capsomeres, provide a basis for icosahedral T = 4 and T = 3 architecture assemblies. These findings advance understanding of honeybee-infecting viruses that can cause Colony Collapse Disorder. Nature Publishing Group UK 2023-02-01 /pmc/articles/PMC9892032/ /pubmed/36726015 http://dx.doi.org/10.1038/s41467-023-36235-3 Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) . |
spellingShingle | Article Chen, Nai-Chi Wang, Chun-Hsiung Yoshimura, Masato Yeh, Yi-Qi Guan, Hong-Hsiang Chuankhayan, Phimonphan Lin, Chien-Chih Lin, Pei-Ju Huang, Yen-Chieh Wakatsuki, Soichi Ho, Meng-Chiao Chen, Chun-Jung Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions |
title | Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions |
title_full | Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions |
title_fullStr | Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions |
title_full_unstemmed | Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions |
title_short | Structures of honeybee-infecting Lake Sinai virus reveal domain functions and capsid assembly with dynamic motions |
title_sort | structures of honeybee-infecting lake sinai virus reveal domain functions and capsid assembly with dynamic motions |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9892032/ https://www.ncbi.nlm.nih.gov/pubmed/36726015 http://dx.doi.org/10.1038/s41467-023-36235-3 |
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