Evidence map›Paper›PMID 28416660›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Redefining the essential trafficking pathway for outer membrane lipoproteins.

Marcin Grabowicz, Thomas J Silhavy

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers.

0numbers the graph read from it
0cells of the map it votes in
87citing papers in PubMed
11.2field-weighted citation impact, top 1% 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

87 citing papers in PubMed, 124 citations in OpenAlex.

  1. ThemBio · 2026
    Article
  2. Article
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  4. Review
  5. Article
  6. Co-opting the bacterial lipoprotein pathway for the biosynthesis of lipidated macrocyclic peptides.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  7. Article
  8. Article
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  11. Review
  12. Article
  13. Repurposing a drug to punish carbapenem-resistantProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Review
  15. Article
  16. Novel Antibacterial Approaches and Therapeutic Strategies.Antibiotics (Basel, Switzerland) · 2025
    Review
  17. Article
  18. The BfmRS stress response protectsJournal of bacteriology · 2025
    Article
  19. Review
  20. Identification and characterization of the lipoproteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article

27 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Marcin GrabowiczDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544.
Thomas J SilhavyDepartment of Molecular Biology, Princeton University, Princeton, NJ 08544 tsilhavy@princeton.edu.
Princeton University · US

Funding

Biogenesis and maintenance of the outer membrane of Gram-negative bacteriaR35GM118024 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 2016 to 2025
$8.1M
GENETIC ANALYSIS OF PROTEIN EXPORTR01GM034821 · NIGMS · PRINCETON UNIVERSITY · PI SILHAVY, THOMAS J. · 1985 to 2015
$4.7M
NIGMS NIH HHS R01 GM034821NIGMS NIH HHS R35 GM118024
6 · The paper itself

Abstract

The outer membrane (OM) of Gram-negative bacteria is a permeability barrier and an intrinsic antibiotic resistance factor. Lipoproteins are OM components that function in cell wall synthesis, diverse secretion systems, and antibiotic efflux pumps. Moreover, each of the essential OM machines that assemble the barrier requires one or more lipoproteins. This dependence is thought to explain the essentiality of the periplasmic chaperone LolA and its OM receptor LolB that traffic lipoproteins to the OM. However, we show that in strains lacking substrates that are toxic when mislocalized, both LolA and LolB can be completely bypassed by activating an envelope stress response without compromising trafficking of essential lipoproteins. We identify the Cpx stress response as a monitor of lipoprotein trafficking tasked with protecting the cell from mislocalized lipoproteins. Moreover, our findings reveal that an alternate trafficking pathway exists that can, under certain conditions, bypass the functions of LolA and LolB, implying that these proteins do not perform any truly essential mechanistic steps in lipoprotein trafficking. Instead, these proteins' key function is to prevent lethal accumulation of mislocalized lipoproteins.

Indexed as

Bacterial Outer Membrane ProteinsCarrier ProteinsEscherichia coliEscherichia coli ProteinsMolecular ChaperonesPeriplasmic Binding ProteinsProtein TransportBacterial Outer Membrane ProteinsCarrier ProteinsEscherichia coli ProteinsLolA protein, E coliLolB protein, E coliMolecular ChaperonesPeriplasmic Binding ProteinsCpx responselipoprotein traffickingLol pathwayNlpEouter membrane

Identifiers

PMID28416660
PMCPMC5422772
OpenAlexW2606101925

What OpenQuestion holds

Textmetadata
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.