Evidence map›Paper›PMID 32367070›Full record

ArticleNature structural & molecular biology2020

Structure of a proton-dependent lipid transporter involved in lipoteichoic acids biosynthesis.

Bing Zhang, Xue Liu, Elisabeth Lambert, Guillaume Mas, Sebastian Hiller, Jan-Willem Veening, Camilo Perez

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
5.0field-weighted citation impact, top 4% of its field
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

28 citing papers in PubMed, 45 citations in OpenAlex.

  1. Article
  2. Review
  3. SpbR controls lipoteichoic acid length by directly inhibiting signal peptidase SpsB inProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Sugar-sensing swodkoreceptors and swodkocrine signaling.Animal models and experimental medicine · 2025
    Article
  5. MprF fromScience advances · 2025
    Article
  6. Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  7. Structure and function ofProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. How to measure omega-3 fatty acid lysolipid flipping: The ultimate guide.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  17. Mfsd2a utilizes a flippase mechanism to mediate omega-3 fatty acid lysolipid transport.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Lipid Transport Across Bacterial Membranes.Annual review of cell and developmental biology · 2022
    Review
  19. Article
  20. Structure and Mechanism of the Lipid Flippase MurJ.Annual review of biochemistry · 2022
    Review
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

7 authors at 2 institutions in 1 country.

Bing Zhang *Biozentrum, University of Basel, Basel, Switzerland.
Xue Liu *Department of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.
Elisabeth Lambert *Biozentrum, University of Basel, Basel, Switzerland.
Guillaume MasBiozentrum, University of Basel, Basel, Switzerland.
Sebastian HillerBiozentrum, University of Basel, Basel, Switzerland.ORCID http://orcid.org/0000-0002-6709-4684
Jan-Willem VeeningDepartment of Fundamental Microbiology, Faculty of Biology and Medicine, University of Lausanne, Lausanne, Switzerland.ORCID http://orcid.org/0000-0002-3162-6634
Camilo PerezBiozentrum, University of Basel, Basel, Switzerland. camilo.perez@unibas.ch.ORCID http://orcid.org/0000-0002-5800-0084
University of Basel · CHUniversity of Lausanne · CH

Funding

European Research Council 771534Swiss National Science Foundation 170607Swiss National Science Foundation 172861
6 · The paper itself

Abstract

Lipoteichoic acids (LTAs) are essential cell-wall components in Gram-positive bacteria, including the human pathogen Staphylococcus aureus, contributing to cell adhesion, cell division and antibiotic resistance. Genetic evidence has suggested that LtaA is the flippase that mediates the translocation of the lipid-linked disaccharide that anchors LTA to the cell membrane, a rate-limiting step in S. aureus LTA biogenesis. Here, we present the structure of LtaA, describe its flipping mechanism and show its functional relevance for S. aureus fitness. We demonstrate that LtaA is a proton-coupled antiporter flippase that contributes to S. aureus survival under physiological acidic conditions. Our results provide foundations for the development of new strategies to counteract S. aureus infections.

Indexed as

Bacterial ProteinsCarrier ProteinsCrystallography, X-RayDiglyceridesDisaccharidesHydrogen-Ion ConcentrationHydrophobic and Hydrophilic InteractionsLipopolysaccharidesMagnetic Resonance SpectroscopyMutationProtein ConformationProtonsStaphylococcus aureusStress, PhysiologicalTeichoic AcidsBacterial ProteinsCarrier ProteinsDiglyceridesDisaccharideslipid transfer proteinLipopolysaccharideslipoteichoic acidProtonsTeichoic Acids

Identifiers

PMID32367070
PMCPMC7611249
OpenAlexW3020880373

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

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.