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Structural Insights into Common and Host-Specific Receptor-Binding Mechanisms in Algal Picorna-like Viruses
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.ORCID iD: 0000-0002-6445-2095
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics. DESY, Ctr Free Electron Laser Sci CFEL, D-22607 Hamburg, Germany..ORCID iD: 0000-0002-5510-2245
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular biophysics.
Japan Fisheries Res & Educ Agcy, Fisheries Technol Inst, Hiroshima 7390452, Japan..
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2022 (English)In: Viruses, E-ISSN 1999-4915, Vol. 14, no 11, article id 2369Article in journal (Refereed) Published
Abstract [en]

Marnaviridae viruses are abundant algal viruses that regulate the dynamics of algal blooms in aquatic environments. They employ a narrow host range because they merely lyse their algal host species. This host-specific lysis is thought to correspond to the unique receptor-binding mechanism of the Marnaviridae viruses. Here, we present the atomic structures of the full and empty capsids of Chaetoceros socialis forma radians RNA virus 1 built-in 3.0 Å and 3.1 Å cryo-electron microscopy maps. The empty capsid structure and the structural variability provide insights into its assembly and uncoating intermediates. In conjunction with the previously reported atomic model of the Chaetoceros tenuissimus RNA virus type II capsid, we have identified the common and diverse structural features of the VP1 surface between the Marnaviridae viruses. We have also tested the potential usage of AlphaFold2 for structural prediction of the VP1s and a subsequent structural phylogeny for classifying Marnaviridae viruses by their hosts. These findings will be crucial for inferring the host-specific receptor-binding mechanism in Marnaviridae viruses.

Place, publisher, year, edition, pages
MDPI, 2022. Vol. 14, no 11, article id 2369
Keywords [en]
Marnaviridae, algal bloom, algal viruses, icosahedral viruses, ssRNA viruses
National Category
Structural Biology
Identifiers
URN: urn:nbn:se:uu:diva-487745DOI: 10.3390/v14112369ISI: 000881549600001PubMedID: 36366467OAI: oai:DiVA.org:uu-487745DiVA, id: diva2:1707686
Funder
Swedish Research Council, 2018-03387The Swedish Foundation for International Cooperation in Research and Higher Education (STINT), JA2014-5721Swedish Research Council Formas, 2018-00421The Royal Swedish Academy of Sciences, BS2018-0053Available from: 2022-11-01 Created: 2022-11-01 Last updated: 2024-02-14Bibliographically approved
In thesis
1. Structural Decorations in Viruses: Unraveling Acquired Functional Structures in Icosahedral RNA Virus Capsids
Open this publication in new window or tab >>Structural Decorations in Viruses: Unraveling Acquired Functional Structures in Icosahedral RNA Virus Capsids
2024 (English)Doctoral thesis, comprehensive summary (Other academic)
Abstract [en]

Viruses have a profound impact worldwide, posing challenges to animal welfare, agriculture, human health, and the ecosystem. This thesis examines the realm of non-enveloped icosahedral double-stranded (ds)RNA and single-stranded (ss)RNA viruses through three studies. In Paper I, we employed a reverse genetics approach to generate recombinant dsRNA totivirus-like viruses—which negatively impact fisheries and the economy—unraveling the intricate relationships between viral genes and life cycles. Our reverse genetic method has proven essential for generating infectious totivirus-like virus particles, allowing for a nuanced exploration of viral behaviors. Understanding these behaviors has the potential to help in developing effective virus control approaches. In Paper II, we elucidated the previously unknown capsid structure, uncovering the intriguing acquired features of a dsRNA megabirnavirus—Rosellinia necatrix megabirnavirus 1-W779 (RnMBV1)—through cryogenic electron microscopy single-particle analysis. RnMBV1, a fungal virus, has potential applications in controlling white root rot, a plant disease that causes substantial economic losses. Insights into this viral structural information can enhance our ability to leverage this fungal virus for economic and agricultural benefits. In Paper III, we obtained the capsid atomic models of a Marnaviridae ssRNA virus: Chaetoceros socialis forma radians RNA virus 1. Additionally, we generated a structure-based phylogeny using viral protein structures predicted by AlphaFold2; this was done to enhance our understanding of algal virus-host specificity. As harmful algal blooms (HABs) pose global threats to ecology and the economy, Chaetoceros algae have emerged as a contributing factor. Certain Marnaviridae viruses exhibit specific infection patterns in Chaetoceros, thereby influencing the occurrence and mitigation of HABs. Studies on Marnaviridae viruses collectively provide insights into the interactions between algal viruses and their hosts, paving the way for utilizing marine algal viruses to address HAB-related challenges. Together, our functional and structural analyses will contribute to a broader understanding of both dsRNA and ssRNA viruses, their behaviors, and their potential applications in addressing economic, agricultural, ecological, and healthcare issues.

Place, publisher, year, edition, pages
Uppsala: Acta Universitatis Upsaliensis, 2024. p. 69
Series
Digital Comprehensive Summaries of Uppsala Dissertations from the Faculty of Science and Technology, ISSN 1651-6214 ; 2364
Keywords
Viruses, RNA viruses, capsid, structure, cryo-EM
National Category
Structural Biology
Research subject
Molecular Life Sciences
Identifiers
urn:nbn:se:uu:diva-523070 (URN)978-91-513-2035-9 (ISBN)
Public defence
2024-04-09, room A1:111a, BMC, Husargatan 3, Uppsala, 13:15 (English)
Opponent
Supervisors
Available from: 2024-03-08 Created: 2024-02-13 Last updated: 2024-03-08Bibliographically approved

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Wang, HanMunke, AnnaOkamoto, Kenta

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