Evidence map›Paper›PMID 39638236›Full record

ArticleJournal of molecular biology2025

Phospholipid Transport Across the Bacterial Periplasm Through the Envelope-spanning Bridge YhdP.

Benjamin F Cooper, Robert Clark, Anju Kudhail, Dali Dunn, Qiaoyu Tian, Gira Bhabha, Damian C Ekiert, Syma Khalid, Georgia L Isom

Abstract read
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In one paragraph

Article in Journal of molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

18 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. YdbL directly modulates YdbH-YnbE bridge formation to maintainbioRxiv : the preprint server for biology · 2026
    Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Bacterial AsmA Proteins Transfer Glycerophospholipids Between MembranesContact (Thousand Oaks (Ventura County, Calif.))
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

9 authors.

Benjamin F CooperSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Robert ClarkDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Anju KudhailSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Dali DunnSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Qiaoyu TianSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK.
Gira BhabhaDepartment of Biology, Johns Hopkins University, Baltimore, MD, United States.
Damian C EkiertDepartment of Biology, Johns Hopkins University, Baltimore, MD, United States.
Syma KhalidDepartment of Biochemistry, University of Oxford, Oxford OX1 3QU, UK.
Georgia L IsomSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, UK. Electronic address: Georgia.Isom@path.ox.ac.uk.

Funding

Unravelling lipid trafficking for the bacterial outer membraneR35GM128777 · NIGMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI Damian Ekiert · 2018 to 2026
$4.1M
Medical Research Council MR/N013468/1Medical Research Council MR/W006731/1Medical Research Council MR/W016672/1NIGMS NIH HHS R35 GM128777
6 · The paper itself

Abstract

The outer membrane of Gram-negative bacteria provides a formidable barrier, essential for both pathogenesis and antimicrobial resistance. Biogenesis of this complex structure necessitates the transport of phospholipids across the cell envelope. Recently, YhdP was implicated as a major protagonist in the trafficking of inner membrane phospholipids to the outer membrane; however the molecular mechanism of YhdP mediated transport remains elusive. Here, utilising AlphaFold, we observe YhdP to form an elongated assembly of 60 β-strands that curve to form a continuous hydrophobic groove. This architecture is consistent with our negative stain electron microscopy data which reveals YhdP to be approximately 250 Å in length and thus sufficient to span the bacterial cell envelope. Furthermore, molecular dynamics simulations and bacterial growth assays indicate essential helical regions at the N- and C-termini of YhdP, that may embed into the inner and outer membranes respectively, reinforcing its envelope spanning nature. Our in vivo crosslinking data reveal phosphate-containing substrates captured along the length of the YhdP groove, providing direct evidence that YhdP interacts with a phosphate-containing substrate, which we propose to be phospholipids. This finding is congruent with our molecular dynamics simulations which demonstrate the propensity for inner membrane lipids to spontaneously enter the groove of YhdP. Collectively, our results support a model in which YhdP bridges the cell envelope, providing a hydrophobic environment for the transport of phospholipids to the outer membrane.

Indexed as

Escherichia coli ProteinsPeriplasmPhospholipidsBacterial Outer MembraneBiological TransportCell MembraneEscherichia coliMolecular Dynamics SimulationEscherichia coli ProteinsPhospholipidsantimicrobial resistancebacterial cell envelopephospholipid transportYhdP

Identifiers

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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.