Evidence map›Paper›PMID 41315346›Full record

ArticleNature communications2025

Structural insights into mechanisms of zinc scavenging by the Candida albicans zincophore Pra1.

Alexandre Nore, Elena Roselletti, Tanmoy Chakraborty, Nicha Särkkä, Rajika L Perera, Duncan Wilson, Johanna L Syrjänen

Abstract read
In one paragraph

Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed, 1 pooled it
–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

2 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

Alexandre NoreFaculty of Health and Life Sciences, Medical Research Council Center for Medical Mycology, Geoffrey Pope Building, University of Exeter, Exeter, UK.
Elena RosellettiFaculty of Health and Life Sciences, Medical Research Council Center for Medical Mycology, Geoffrey Pope Building, University of Exeter, Exeter, UK.
Tanmoy ChakrabortyFaculty of Health and Life Sciences, Medical Research Council Center for Medical Mycology, Geoffrey Pope Building, University of Exeter, Exeter, UK.
Nicha SärkkäInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland.
Rajika L PereraPoseidon Laboratory, Pasadena, CA, USA.ORCID http://orcid.org/0000-0002-4932-8168
Duncan WilsonFaculty of Health and Life Sciences, Medical Research Council Center for Medical Mycology, Geoffrey Pope Building, University of Exeter, Exeter, UK. duncan.wilson@exeter.ac.uk.ORCID http://orcid.org/0000-0001-6617-0123
Johanna L SyrjänenInstitute of Biotechnology, HiLIFE, University of Helsinki, Helsinki, Finland. johanna.syrjanen@helsinki.fi.

Funding

ChimeraX -- Next Generation Visualization and Analysis Software for Multiscale ModelingR01GM129325 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI FERRIN, THOMAS E · 2018 to 2025
$5.2M
NIGMS NIH HHS R01 GM129325Wellcome TrustWellcome Trust (Wellcome) 214317/A/18/Z
6 · The paper itself

Abstract

Candida albicans causes over 400,000 life-threatening, and an additional half a billion of mucosal infections annually. In response to infection, the host limits essential micronutrient availability, including zinc, to restrict growth of the invading pathogen. As assimilation of zinc is essential for C. albicans pathogenicity, limitation induces secretion of the zincophore protein Pra1 to scavenge zinc from the host. Pra1 also plays a number of important roles in host-pathogen interactions and is conserved in most fungi. However, the structure of fungal zincophores is unknown. Here, we present cryo-EM structures of C. albicans Pra1 in apo- and zinc-bound states, at 2.8 and 2.5 Å resolution respectively. Our work reveals a hexameric ring with multiple zinc binding sites. Through genetic studies, we show that these sites are essential for C. albicans growth under zinc restriction but do not affect the inflammatory properties of Pra1. These data create a foundation for future work to explore the structural basis of Pra1-mediated host-pathogen interactions, C. albicans zinc uptake, as well as therapeutics development.

Indexed as

Candida albicansFungal ProteinsZincAnimalsBinding SitesCryoelectron MicroscopyHost-Pathogen InteractionsModels, MolecularProtein BindingFungal ProteinsZinc

Identifiers

PMID41315346
PMCPMC12663325

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

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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.