Evidence map›Paper›PMID 41644548›Full record

ArticleNature communications2026

Molecular insights into the capsular polysaccharide transporter Wza-Wzc complex.

Biao Yuan, Christian Sieben, Prateek Raj, Tina Rietschel, Rory Hennell James, Anja Gatzemeier, Lothar Jänsch, Thomas C Marlovits, Dirk W Heinz

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. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing 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

6 citing papers in PubMed.

  1. Hypermucoviscosity inJournal of bacteriology · 2026
    Review
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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

9 authors.

Biao YuanDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany. biao.yuan@helmholtz-hzi.de.ORCID http://orcid.org/0000-0002-7137-6270
Christian SiebenNanoscale Infection Biology Group, Department of Cell Biology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany.ORCID http://orcid.org/0000-0002-2836-2623
Prateek RajDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany.
Tina RietschelCellular Proteome Research Group, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany.ORCID http://orcid.org/0009-0009-1339-9827
Rory Hennell JamesInstitute for Microbial and Molecular Sciences, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany.ORCID http://orcid.org/0000-0001-9009-9726
Anja GatzemeierDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany.
Lothar JänschCellular Proteome Research Group, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany.
Thomas C MarlovitsInstitute for Microbial and Molecular Sciences, University Medical Center Hamburg-Eppendorf (UKE), Hamburg, Germany.ORCID http://orcid.org/0000-0001-8106-4038
Dirk W HeinzDepartment of Molecular Structural Biology, Helmholtz Centre for Infection Research (HZI), Braunschweig, Germany. dirk.heinz@helmholtz-hzi.de.ORCID http://orcid.org/0009-0006-0514-1728

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Capsular polysaccharides (CPS) are key virulence determinants, constituting the protective capsule that surrounds bacterial pathogens. Here, we present the complete cryo-EM structure of Gram-negative bacterial CPS secretion machinery formed by the E. coli K12 Wza-Wzc complex. The structure reveals an elongated, continuous channel spanning the entire envelope that facilitates CPS secretion. Multiple structural snapshots of the ADP-bound Wza-Wzc complex capture intermediate conformations of the double membrane assembly, highlighting its remarkable intrinsic dynamics. In-depth analysis of the isolated Wza translocon and Wzc co-polymerase, reveals mechanistic details of both complex formation and CPS transport. We further uncover the jellyroll domain of Wzc as a CPS-binding module, likely guiding CPS repeat units into a proposed Wzc-Wzy polymerization platform. Collectively, this work provides structural and functional insights into CPS synthesis and transport, advancing our understanding of bacterial capsule formation and virulence mechanisms.

Indexed as

Bacterial CapsulesEscherichia coli K12Escherichia coli ProteinsMembrane Transport ProteinsPolysaccharides, BacterialCryoelectron MicroscopyModels, MolecularEscherichia coli ProteinsMembrane Transport ProteinsPolysaccharides, Bacterial

Identifiers

PMID41644548
PMCPMC12881504

What OpenQuestion holds

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LicenceCC BY
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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.