Evidence map›Paper›PMID 42069710›Full record

ArticleNature communications2026

Structural basis for transport and inhibition of nucleotide sugar transport in pathogenic fungi.

Joanne L Parker, Justin C Deme, Bjarne Feddersen, Susan M Lea, Simon Newstead

Abstract read
In one paragraph

Article in Nature communications, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors.

Joanne L Parker *Department of Biochemistry, University of Oxford, Oxford, UK. joanne.parker@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0003-2964-2720
Justin C Deme *Center for Structural Biology, Center for Cancer Research, National Cancer Institute, Frederick, MD, USA.
Bjarne FeddersenDepartment of Biochemistry, University of Oxford, Oxford, UK.ORCID http://orcid.org/0000-0003-4503-3343
Susan M LeaCenter for Structural Biology, Center for Cancer Research, National Cancer Institute, Frederick, MD, USA. susan.lea@stjude.org.ORCID http://orcid.org/0000-0001-9287-8053
Simon NewsteadDepartment of Biochemistry, University of Oxford, Oxford, UK. simon.newstead@bioch.ox.ac.uk.ORCID http://orcid.org/0000-0001-7432-2270

Funding

RCUK | Medical Research Council (MRC) MR/S021043/1Wellcome Trust (Wellcome) 219531/Z/19/Z
6 · The paper itself

Abstract

GDP-Mannose transporters are Golgi-localised solute carriers that are essential for the virulence of pathogenic fungi, serving as critical components of fungal glycosylation pathways. However, the mechanism by which nucleotide sugars are recognised and transported across the Golgi membrane remains unclear, hindering efforts to develop effective inhibitors that could serve as distinct antifungal agents. Here, we present cryo-EM structures of the GDP-Mannose transporter, Vrg4, from Candida albicans in complex with nanobodies in both the cytoplasmic and Golgi-facing states. Structural comparisons between these two states, in addition to a GDP-mannose bound structure, demonstrate the importance of ligand movement during transport. Additionally, we demonstrate the ability of the nanobodies to specifically inhibit Vrg4, presenting proof-of-principle that nanobodies can be used as effective inhibitors of nucleotide sugar transport and glycosylation in cells.

Indexed as

Candida albicansFungal ProteinsBiological TransportCryoelectron MicroscopyGlycosylationGolgi ApparatusGuanosine Diphosphate MannoseNucleotidesFungal ProteinsGuanosine Diphosphate MannoseNucleotides

Identifiers

PMID42069710
PMCPMC13342644

What OpenQuestion holds

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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.