Evidence map›Paper›PMID 22354022›Full record

ArticleInfection and immunity2012

Loss of outer membrane protein C in Escherichia coli contributes to both antibiotic resistance and escaping antibody-dependent bactericidal activity.

Yi-Fang Liu, Jing-Jou Yan, Huan-Yao Lei, Ching-Hao Teng, Ming-Cheng Wang, Chin-Chung Tseng, Jiunn-Jong Wu

Open access · bronzeAbstract read
In one paragraph

Article in Infection and immunity, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

57 citing papers in PubMed, 110 citations in OpenAlex.

  1. Biofilm Formation and the Pore ProteinsAntibiotics (Basel, Switzerland) · 2026
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  3. Review
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  5. Mechanisms ofMicroorganisms · 2025
    Article
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  7. Article
  8. Article
  9. International journal of molecular sciences · 2024
    Article
  10. Upregulation of outer membrane porin geneMicrobiology spectrum · 2024
    Article
  11. Article
  12. Article
  13. Fosfomycin Uptake inACS infectious diseases · 2024
    Article
  14. Nanopore sequencing elucidatesAccess microbiology · 2024
    Article
  15. Article
  16. An elevated OmpA expression during the production of a recombinant protein in Escherichia coli.Brazilian journal of microbiology : [publication of the Brazilian Society for Microbiology] · 2023
    Article
  17. Article
  18. Review
  19. Article
  20. Article
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 1 institution in 1 country.

Yi-Fang LiuInstitutes of Basic Medical Sciences, National Cheng-Kung University, Tainan, Taiwan.
Jing-Jou Yan
Huan-Yao Lei
Ching-Hao Teng
Ming-Cheng Wang
Chin-Chung Tseng
Jiunn-Jong Wu
National Cheng Kung University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Outer membrane proteins (OMPs) serve as the permeability channels for nutrients, toxins, and antibiotics. In Escherichia coli, OmpA has been shown to be involved in bacterial virulence, and OmpC is related to multidrug resistance. However, it is unclear whether OmpC also has a role in the virulence of E. coli. The aims of this study were to characterize the role of OmpC in antimicrobial resistance and bacterial virulence in E. coli. The ompC deletion mutant showed significantly decreased susceptibility to carbapenems and cefepime. To investigate the survival of E. coli exposed to the innate immune system, a human blood bactericidal assay showed that the ompC mutant increased survival in blood and serum but not in complement-inactivated serum. These effects were also demonstrated in the natural selection of OmpC mutants. Also, C1q interacted with E. coli through a complex of antibodies bound to OmpC as a major target. Bacterial survival was increased in the wild-type strain in a dose-dependent manner by adding free recombinant OmpC protein or anti-C1q antibody to human serum. These results demonstrated that the interaction of OmpC-specific antibody and C1q was the key step in initiating the antibody-dependent classical pathway for the clearance of OmpC-expressing E. coli. Anti-OmpC antibody was detected in human sera, indicating that OmpC is an immunogen. These data indicate that the loss of OmpC in E. coli is resistant to not only antibiotics, but also the serum bactericidal effect, which is mediated from the C1q and anti-OmpC antibody-dependent classical pathway.

Indexed as

AnimalsAnti-Bacterial AgentsAntibodies, BacterialAntibody SpecificityAntigens, BacterialComplement C1qDrug Resistance, BacterialEscherichia coliGene Expression Regulation, BacterialGenotypeHumansMiceMice, Inbred BALB CMutationPorinsRecombinant ProteinsAnti-Bacterial AgentsAntibodies, BacterialAntigens, BacterialComplement C1qOmpC proteinPorinsRecombinant Proteins

Identifiers

PMID22354022
PMCPMC3347438
OpenAlexW2138064018

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.