Evidence map›Paper›PMID 41042861›Full record

ArticleScience advances2025

Cryo-EM resolves the structure of the archaeal dsDNA virus HFTV1 from head to tail.

Daniel X Zhang, Michail N Isupov, Rebecca M Davies, Sabine Schwarzer, Mathew McLaren, William S Stuart, Vicki A M Gold, Hanna M Oksanen, Tessa E F Quax, Bertram Daum

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

7 citing papers in PubMed.

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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

10 authors.

Daniel X ZhangLiving Systems Institute, University of Exeter, Exeter EX4 4QD, UK.ORCID 0009-0000-3708-5288
Michail N IsupovHenry Wellcome Building for Biocatalysis, Biosciences, Faculty of Health and Life Sciences, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0001-6842-4289
Rebecca M DaviesLiving Systems Institute, University of Exeter, Exeter EX4 4QD, UK.ORCID 0009-0008-6564-7637
Sabine SchwarzerDepartment of Molecular Microbiology, Groningen Biomolecular Sciences & Biotechnology Institute, Faculty for Science and Engineering, University of Groningen, 9747 AG Groningen, Netherlands.ORCID 0000-0003-2534-8049
Mathew McLarenLiving Systems Institute, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0002-6636-7409
William S StuartLiving Systems Institute, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0002-5560-1167
Vicki A M GoldLiving Systems Institute, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0002-6908-0745
Hanna M OksanenMolecular and Integrative Biosciences Research Programme, Faculty of Biology and Environmental Sciences, University of Helsinki, Viikinkaari 9, 00014 Helsinki, Finland.ORCID 0000-0003-3047-8294
Tessa E F QuaxDepartment of Molecular Microbiology, Groningen Biomolecular Sciences & Biotechnology Institute, Faculty for Science and Engineering, University of Groningen, 9747 AG Groningen, Netherlands.ORCID 0000-0001-5516-5871
Bertram DaumLiving Systems Institute, University of Exeter, Exeter EX4 4QD, UK.ORCID 0000-0002-3767-264X

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While archaeal viruses show a stunning diversity of morphologies, many bear a notable resemblance to tailed bacterial phages. This raises fundamental questions: Do all tailed viruses share a common origin and do they infect their hosts in similar ways? Answering these questions requires high-resolution structural insights, yet no complete atomic models of archaeal viruses have been available. Here, we present the near-atomic resolution structure of Haloferax tailed virus 1 (HFTV1), an archaeal virus thriving in extreme salinity. Using cryo-electron microscopy, we resolve the architecture and assembly of all structural proteins and capture conformational transitions associated with DNA ejection. Our data reveal genome spooling within the capsid and identify putative receptor-binding and catalytic sites for host recognition and infection. These findings uncover key mechanisms of archaeal virus assembly, principles of virus-host interactions, and evolutionary links connecting archaeal, bacterial, and eukaryotic viruses.

Indexed as

Archaeal VirusesCryoelectron MicroscopyDNA VirusesArchaeaCapsidGenome, ViralModels, Molecular

Identifiers

PMID41042861
PMCPMC12494034

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.