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Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles
The coat proteins (CPs) of single-stranded RNA bacteriophages (ssRNA phages) directly assemble around the genomic RNA (gRNA) to form a near-icosahedral capsid with a single maturation protein (Mat) that binds the gRNA and interacts with the retractile pilus during infection of the host. Understandin...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880383/ https://www.ncbi.nlm.nih.gov/pubmed/35215818 http://dx.doi.org/10.3390/v14020225 |
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author | Chang, Jeng-Yih Gorzelnik, Karl V. Thongchol, Jirapat Zhang, Junjie |
author_facet | Chang, Jeng-Yih Gorzelnik, Karl V. Thongchol, Jirapat Zhang, Junjie |
author_sort | Chang, Jeng-Yih |
collection | PubMed |
description | The coat proteins (CPs) of single-stranded RNA bacteriophages (ssRNA phages) directly assemble around the genomic RNA (gRNA) to form a near-icosahedral capsid with a single maturation protein (Mat) that binds the gRNA and interacts with the retractile pilus during infection of the host. Understanding the assembly of ssRNA phages is essential for their use in biotechnology, such as RNA protection and delivery. Here, we present the complete gRNA model of the ssRNA phage Qβ, revealing that the 3′ untranslated region binds to the Mat and the 4127 nucleotides fold domain-by-domain, and is connected through long-range RNA–RNA interactions, such as kissing loops. Thirty-three operator-like RNA stem-loops are located and primarily interact with the asymmetric A/B CP-dimers, suggesting a pathway for the assembly of the virions. Additionally, we have discovered various forms of the virus-like particles (VLPs), including the canonical T = 3 icosahedral, larger T = 4 icosahedral, prolate, oblate forms, and a small prolate form elongated along the 3-fold axis. These particles are all produced during a normal infection, as well as when overexpressing the CPs. When overexpressing the shorter RNA fragments encoding only the CPs, we observed an increased percentage of the smaller VLPs, which may be sufficient to encapsidate a shorter RNA. |
format | Online Article Text |
id | pubmed-8880383 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-88803832022-02-26 Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles Chang, Jeng-Yih Gorzelnik, Karl V. Thongchol, Jirapat Zhang, Junjie Viruses Article The coat proteins (CPs) of single-stranded RNA bacteriophages (ssRNA phages) directly assemble around the genomic RNA (gRNA) to form a near-icosahedral capsid with a single maturation protein (Mat) that binds the gRNA and interacts with the retractile pilus during infection of the host. Understanding the assembly of ssRNA phages is essential for their use in biotechnology, such as RNA protection and delivery. Here, we present the complete gRNA model of the ssRNA phage Qβ, revealing that the 3′ untranslated region binds to the Mat and the 4127 nucleotides fold domain-by-domain, and is connected through long-range RNA–RNA interactions, such as kissing loops. Thirty-three operator-like RNA stem-loops are located and primarily interact with the asymmetric A/B CP-dimers, suggesting a pathway for the assembly of the virions. Additionally, we have discovered various forms of the virus-like particles (VLPs), including the canonical T = 3 icosahedral, larger T = 4 icosahedral, prolate, oblate forms, and a small prolate form elongated along the 3-fold axis. These particles are all produced during a normal infection, as well as when overexpressing the CPs. When overexpressing the shorter RNA fragments encoding only the CPs, we observed an increased percentage of the smaller VLPs, which may be sufficient to encapsidate a shorter RNA. MDPI 2022-01-24 /pmc/articles/PMC8880383/ /pubmed/35215818 http://dx.doi.org/10.3390/v14020225 Text en © 2022 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Chang, Jeng-Yih Gorzelnik, Karl V. Thongchol, Jirapat Zhang, Junjie Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles |
title | Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles |
title_full | Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles |
title_fullStr | Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles |
title_full_unstemmed | Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles |
title_short | Structural Assembly of Qβ Virion and Its Diverse Forms of Virus-like Particles |
title_sort | structural assembly of qβ virion and its diverse forms of virus-like particles |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8880383/ https://www.ncbi.nlm.nih.gov/pubmed/35215818 http://dx.doi.org/10.3390/v14020225 |
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