Evidence map›Paper›PMID 40751015›Full record

ArticleNature microbiology2025

Metal-induced conformational changes in the Sabiá virus spike complex.

Hadas Cohen-Dvashi, Michael Katz, Ron Diskin

Abstract read
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In one paragraph

Article in Nature microbiology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Modeling Alternative Conformational States in CASP16.bioRxiv : the preprint server for biology · 2025
    Article
  5. Article
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

3 authors.

Hadas Cohen-DvashiDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Michael KatzDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel.
Ron DiskinDepartment of Chemical and Structural Biology, Weizmann Institute of Science, Rehovot, Israel. ron.diskin@weizmann.ac.il.ORCID http://orcid.org/0000-0002-2837-5897

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Haemorrhagic fever viruses from the Arenaviridae are a source of concern owing to their potential to cause lethal outbreaks and the lack of effective therapeutics. While structures of spike proteins from 'Old World' arenaviruses are available, the differences and similarities to 'New World' arenaviruses, such as the Sabiá virus, remain unclear owing to the lack of New World spike structures. Here we present the structure of the isolated spike complex from the Sabiá virus, which mediates viral attachment and entry to the host cells, using single-particle cryo-electron microscopy. We find two distinct conformational states of the spike, representing its native closed state at 2.6 Å resolution and an open state at 2.9 Å resolution that it assumes during cell entry. In addition, we show that the opening of the spike and subsequent cell entry are dependent on acidic pH and an unidentified metal ion. Our study suggests potential differences in the cell entry mechanisms of clade B arenaviruses compared with others in the Arenaviridae family.

Indexed as

Arenaviruses, New WorldMetalsAnimalsCryoelectron MicroscopyHumansHydrogen-Ion ConcentrationModels, MolecularProtein ConformationVirus InternalizationMetals

Identifiers

What OpenQuestion holds

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Registered trials

None linked

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.