Evidence map›Paper›PMID 34781743›Full record

ArticlemBio2021

YhdP, TamB, and YdbH Are Redundant but Essential for Growth and Lipid Homeostasis of the Gram-Negative Outer Membrane.

Natividad Ruiz, Rebecca M Davis, Sujeet Kumar

Open access · goldAbstract read
In one paragraph

Article in mBio, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
9.4field-weighted citation impact, top 2% 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

60 citing papers in PubMed, 81 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. YdbL directly modulates YdbH-YnbE bridge formation to maintainbioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. A surface-exposed cardiolipin synthase provides an unexpected paradigm for maintaining the Gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  11. Article
  12. Article
  13. Article
  14. Control of theJournal of bacteriology · 2025
    Article
  15. Article
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  17. Article
  18. 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

3 authors at 1 institution in 1 country.

Natividad RuizDepartment of Microbiology, The Ohio State Universitygrid.261331.4, Columbus, Ohio, USA.ORCID 0000-0002-6369-2206
Rebecca M DavisDepartment of Microbiology, The Ohio State Universitygrid.261331.4, Columbus, Ohio, USA.
Sujeet KumarDepartment of Microbiology, The Ohio State Universitygrid.261331.4, Columbus, Ohio, USA.
The Ohio State University · US

Funding

Envelope Biogenesis in Gram-negative BacteriaR01GM100951 · NIGMS · OHIO STATE UNIVERSITY · PI RUIZ, NATIVIDAD · 2012 to 2023
$3.7M
Functional characterization of AsmA-like proteins in Escherichia coliR03AI139271 · NIAID · OHIO STATE UNIVERSITY · PI RUIZ, NATIVIDAD · 2018 to 2019
$156k
NIAID NIH HHS R03 AI139271NIGMS NIH HHS R01 GM100951
6 · The paper itself

Abstract

The bacterial cell envelope is the first line of defense and point of contact with the environment and other organisms. Envelope biogenesis is therefore crucial for the survival and physiology of bacteria and is often targeted by antimicrobials. Gram-negative bacteria have a multilayered envelope delimited by an inner and outer membrane (IM and OM, respectively). The OM is a barrier against many antimicrobials because of its asymmetric lipid structure, with phospholipids composing the inner leaflet and lipopolysaccharides (LPS) the outer leaflet. Since lipid synthesis occurs at the IM, phospholipids and LPS are transported across the cell envelope and asymmetrically assembled at the OM during growth. How phospholipids are transported to the OM remains unknown. Recently, the Escherichia coli protein YhdP has been proposed to participate in this process through an unknown mechanism. YhdP belongs to the AsmA-like clan and contains domains homologous to those found in lipid transporters. Here, we used genetics to investigate the six members of the AsmA-like clan of proteins in E. coli. Our data show that YhdP and its paralogs TamB and YdbH are redundant, but not equivalent, in performing an essential function in the cell envelope. Among the AsmA-like paralogs, only the combined loss of YhdP, TamB, and YdbH is lethal, and any of these three proteins is sufficient for growth. We also show that these proteins are required for OM lipid homeostasis and propose that they are the long-sought-after phospholipid transporters that are required for OM biogenesis.

Indexed as

Lipid MetabolismBacterial Outer MembraneEscherichia coliEscherichia coli ProteinsHomeostasisMembrane LipidsMembrane ProteinsEscherichia coli ProteinsMembrane LipidsMembrane ProteinsYhdP protein, E coliAsmA-like proteinsenvelope biogenesisouter membrane biogenesisphospholipid transportsynthetic lethality

Identifiers

PMID34781743
PMCPMC8593681
OpenAlexW3211552303

What OpenQuestion holds

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LicenceCC BY
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.