Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling
Gespeichert in:
| Titel: | Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling |
|---|---|
| Autoren: | Gebhard, L. Johanna, Tomaru, Yuji, Okamoto, Kenta, Munke, Anna |
| Weitere Verfasser: | Lund University, Faculty of Science, Department of Chemistry, Center for Molecular Protein Science, Biochemistry and Structural Biology, Lunds universitet, Naturvetenskapliga fakulteten, Kemiska institutionen, Centrum för Molekylär Proteinvetenskap, Biokemi och Strukturbiologi, Originator |
| Quelle: | Virology Journal. 22 |
| Schlagwörter: | Natural Sciences, Biological Sciences, Microbiology, Naturvetenskap, Biologi, Mikrobiologi, Structural Biology, Strukturbiologi |
| Beschreibung: | Viruses that infect single-celled algae strongly regulate microalgae growth and community composition through cell lysis, enable nutrient recycling in marine ecosystems, and offer valuable insights into early stages of viral evolution. One major group, the Bacilladnaviridae family of single-stranded DNA viruses, infects diatoms in marine environments. Here, we present the capsid structure of Chaetoceros lorenzianus DNA virus (ClorDNAV, Protobacilladnavirus chaelor) determined at 2.2 Å resolution, thereby expanding the known structural diversity within the Cressdnaviricota phylum. The ClorDNAV capsid protein (CP) contains a conserved jelly-roll fold and a surface-exposed projection domain, with both N- and C-termini oriented toward the capsid interior. A low-resolution reconstruction of the genome revealed a spooled arrangement of the outer DNA layer, similar to that observed in Chaetoceros tenuissimus DNA virus type II (CtenDNAV-II). Structural comparison with CtenDNAV-II revealed five key CP differences: the absence of surface-exposed C-terminal tails in ClorDNAV, the presence of a helical domain, differences in the projection domain conformation, variation in the number of β-strands in the jelly-roll fold, and the lack of ion-attributed densities at subunit interfaces. Together with the genome reconstruction, these findings underscore the importance of experimentally determined structures for understanding viral architecture and evolution. To complement these results, we analyzed AlphaFold3-predicted CPs from all classified Bacilladnaviridae genera. These models confirmed the conservation of the jelly-roll fold across the family while revealing variability in the surface-exposed and terminal regions, likely reflecting host-specific adaptations and genome packaging strategies. Together, the experimental and predicted structures provide a comprehensive view of structural conservation and divergence in Bacilladnaviridae. Furthermore, the results provide additional structural evidence for the evolution of ssDNA Bacilladnaviridae from a noda-like ssRNA virus ancestor and suggest a shared genome organization resembling that of double-stranded viruses. |
| Zugangs-URL: | https://doi.org/10.1186/s12985-025-03019-8 |
| Datenbank: | SwePub |
| FullText | Text: Availability: 0 CustomLinks: – Url: https://doi.org/10.1186/s12985-025-03019-8# Name: EDS - SwePub (s4221598) Category: fullText Text: View record in SwePub – Url: http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=search&db=pmc&term=1743-422X[TA]+AND+[PG]+AND+2025[PDAT] Name: FREE - PubMed Central (ISSN based link) Category: fullText Text: Full Text Icon: https://imageserver.ebscohost.com/NetImages/iconPdf.gif MouseOverText: Check this PubMed for the article full text. – Url: https://resolver.ebscohost.com/openurl?sid=EBSCO:edsswe&genre=article&issn=1743422X&ISBN=&volume=22&issue=&date=20251201&spage=&pages=&title=Virology Journal&atitle=Structural%20diversity%20and%20conservation%20among%20CRESS-DNA%20bacilladnaviruses%20revealed%20through%20cryo-EM%20and%20computational%20modelling&aulast=Gebhard%2C%20L.%20Johanna&id=DOI:10.1186/s12985-025-03019-8 Name: Full Text Finder Category: fullText Text: Full Text Finder Icon: https://imageserver.ebscohost.com/branding/images/FTF.gif MouseOverText: Full Text Finder – Url: https://www.webofscience.com/api/gateway?GWVersion=2&SrcApp=EBSCO&SrcAuth=EBSCO&DestApp=WOS&ServiceName=TransferToWoS&DestLinkType=GeneralSearchSummary&Func=Links&author=Gebhard%20LJ Name: ISI Category: fullText Text: Nájsť tento článok vo Web of Science Icon: https://imagesrvr.epnet.com/ls/20docs.gif MouseOverText: Nájsť tento článok vo Web of Science |
|---|---|
| Header | DbId: edsswe DbLabel: SwePub An: edsswe.oai.portal.research.lu.se.publications.e8d755b3.7d9f.4418.b085.f7c03f36b53c RelevancyScore: 1124 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 1123.91345214844 |
| IllustrationInfo | |
| Items | – Name: Title Label: Title Group: Ti Data: Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Gebhard%2C+L%2E+Johanna%22">Gebhard, L. Johanna</searchLink><br /><searchLink fieldCode="AR" term="%22Tomaru%2C+Yuji%22">Tomaru, Yuji</searchLink><br /><searchLink fieldCode="AR" term="%22Okamoto%2C+Kenta%22">Okamoto, Kenta</searchLink><br /><searchLink fieldCode="AR" term="%22Munke%2C+Anna%22">Munke, Anna</searchLink> – Name: Author Label: Contributors Group: Au Data: Lund University, Faculty of Science, Department of Chemistry, Center for Molecular Protein Science, Biochemistry and Structural Biology, Lunds universitet, Naturvetenskapliga fakulteten, Kemiska institutionen, Centrum för Molekylär Proteinvetenskap, Biokemi och Strukturbiologi, Originator – Name: TitleSource Label: Source Group: Src Data: <i>Virology Journal</i>. 22 – Name: Subject Label: Subject Terms Group: Su Data: <searchLink fieldCode="DE" term="%22Natural+Sciences%22">Natural Sciences</searchLink><br /><searchLink fieldCode="DE" term="%22Biological+Sciences%22">Biological Sciences</searchLink><br /><searchLink fieldCode="DE" term="%22Microbiology%22">Microbiology</searchLink><br /><searchLink fieldCode="DE" term="%22Naturvetenskap%22">Naturvetenskap</searchLink><br /><searchLink fieldCode="DE" term="%22Biologi%22">Biologi</searchLink><br /><searchLink fieldCode="DE" term="%22Mikrobiologi%22">Mikrobiologi</searchLink><br /><searchLink fieldCode="DE" term="%22Structural+Biology%22">Structural Biology</searchLink><br /><searchLink fieldCode="DE" term="%22Strukturbiologi%22">Strukturbiologi</searchLink> – Name: Abstract Label: Description Group: Ab Data: Viruses that infect single-celled algae strongly regulate microalgae growth and community composition through cell lysis, enable nutrient recycling in marine ecosystems, and offer valuable insights into early stages of viral evolution. One major group, the Bacilladnaviridae family of single-stranded DNA viruses, infects diatoms in marine environments. Here, we present the capsid structure of Chaetoceros lorenzianus DNA virus (ClorDNAV, Protobacilladnavirus chaelor) determined at 2.2 Å resolution, thereby expanding the known structural diversity within the Cressdnaviricota phylum. The ClorDNAV capsid protein (CP) contains a conserved jelly-roll fold and a surface-exposed projection domain, with both N- and C-termini oriented toward the capsid interior. A low-resolution reconstruction of the genome revealed a spooled arrangement of the outer DNA layer, similar to that observed in Chaetoceros tenuissimus DNA virus type II (CtenDNAV-II). Structural comparison with CtenDNAV-II revealed five key CP differences: the absence of surface-exposed C-terminal tails in ClorDNAV, the presence of a helical domain, differences in the projection domain conformation, variation in the number of β-strands in the jelly-roll fold, and the lack of ion-attributed densities at subunit interfaces. Together with the genome reconstruction, these findings underscore the importance of experimentally determined structures for understanding viral architecture and evolution. To complement these results, we analyzed AlphaFold3-predicted CPs from all classified Bacilladnaviridae genera. These models confirmed the conservation of the jelly-roll fold across the family while revealing variability in the surface-exposed and terminal regions, likely reflecting host-specific adaptations and genome packaging strategies. Together, the experimental and predicted structures provide a comprehensive view of structural conservation and divergence in Bacilladnaviridae. Furthermore, the results provide additional structural evidence for the evolution of ssDNA Bacilladnaviridae from a noda-like ssRNA virus ancestor and suggest a shared genome organization resembling that of double-stranded viruses. – Name: URL Label: Access URL Group: URL Data: <link linkTarget="URL" linkTerm="https://doi.org/10.1186/s12985-025-03019-8" linkWindow="_blank">https://doi.org/10.1186/s12985-025-03019-8</link> |
| PLink | https://erproxy.cvtisr.sk/sfx/access?url=https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=edsswe&AN=edsswe.oai.portal.research.lu.se.publications.e8d755b3.7d9f.4418.b085.f7c03f36b53c |
| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1186/s12985-025-03019-8 Languages: – Text: English Subjects: – SubjectFull: Natural Sciences Type: general – SubjectFull: Biological Sciences Type: general – SubjectFull: Microbiology Type: general – SubjectFull: Naturvetenskap Type: general – SubjectFull: Biologi Type: general – SubjectFull: Mikrobiologi Type: general – SubjectFull: Structural Biology Type: general – SubjectFull: Strukturbiologi Type: general Titles: – TitleFull: Structural diversity and conservation among CRESS-DNA bacilladnaviruses revealed through cryo-EM and computational modelling Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Gebhard, L. Johanna – PersonEntity: Name: NameFull: Tomaru, Yuji – PersonEntity: Name: NameFull: Okamoto, Kenta – PersonEntity: Name: NameFull: Munke, Anna – PersonEntity: Name: NameFull: Lund University, Faculty of Science, Department of Chemistry, Center for Molecular Protein Science, Biochemistry and Structural Biology, Lunds universitet, Naturvetenskapliga fakulteten, Kemiska institutionen, Centrum för Molekylär Proteinvetenskap, Biokemi och Strukturbiologi, Originator IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 12 Type: published Y: 2025 Identifiers: – Type: issn-print Value: 1743422X – Type: issn-locals Value: SWEPUB_FREE – Type: issn-locals Value: LU_SWEPUB Numbering: – Type: volume Value: 22 Titles: – TitleFull: Virology Journal Type: main |
| ResultId | 1 |
Full Text Finder
Nájsť tento článok vo Web of Science