Evidence map›Paper›PMID 31189981›Full record

ArticleScientific reports2019

Identification of specific protein amino acid substitutions of extended-spectrum β-lactamase (ESBL)-producing Escherichia coli ST131: a proteomics approach using mass spectrometry.

Akihiro Nakamura, Masaru Komatsu, Yuki Ohno, Nobuyoshi Noguchi, Akira Kondo, Naoya Hatano

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed, 1 pooled it
0.8field-weighted citation impact, top 34% 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

12 citing papers in PubMed, 1 synthesis or guideline pooled it, 18 citations in OpenAlex.

  1. Pooled it
  2. A NovelMicroorganisms · 2026
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  7. Review
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  12. The Role of Proteomics in Bacterial Response to Antibiotics.Pharmaceuticals (Basel, Switzerland) · 2020
    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

6 authors at 3 institutions in 1 country.

Akihiro NakamuraDepartment of Clinical Laboratory Science, Faculty of Health Care, Tenri Health Care University, Tenri, Japan. nakamurium@gmail.com.ORCID http://orcid.org/0000-0003-2065-6720
Masaru KomatsuDepartment of Clinical Laboratory Science, Faculty of Health Care, Tenri Health Care University, Tenri, Japan.
Yuki OhnoDepartment of Clinical Bacteriology, Clinical Laboratory Medicine, Tenri Hospital, Tenri, Japan.
Nobuyoshi NoguchiDepartment of Clinical Laboratory Science, Faculty of Health Care, Tenri Health Care University, Tenri, Japan.
Akira KondoDepartment of Clinical Laboratory Science, Faculty of Health Care, Tenri Health Care University, Tenri, Japan.
Naoya HatanoThe Integrated Center for Mass Spectrometry, Kobe University Graduate School of Medicine, Kobe, Japan.
Tenri Health Care University · JPTenri Hospital · JPKobe University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The global pandemic of ESBL-producing Escherichia coli is associated with sequence type 131 (ST131). However, mechanisms of ST131 spread remain unclear. This study searched for proteins with amino acid substitutions specific for ST131 and used proteomics analysis to clarify ST131 characteristics. Five proteins had ST131-specific amino acid substitutions: uncharacterized protein YahO with E34A (m/z 7655); UPF0337 protein YjbJ with V59D, D60S and T63K (m/z 8351); uncharacterized protein YnfD with S106T (m/z 8448); and acid stress chaperone HdeA with Q92K and N94S (m/z 9714). Soluble cytochrome b562 (m/z 11783) showed seven amino acid substitutions, and the sequence differed between clade C of the pandemic clade and non-C. In silico analysis showed YahO protein-protein interaction with YjbJ, possibly related to biofilm formation. Although the function of soluble cytochrome b562 is electron transport of unknown function, its involvement in biofilm formation was predicted. HdeA was a gastric acid resistance-related protein. The function of YnfD was completely unclear. In conclusion, ST131-specific protein amino acid substitutions consisted mainly of a gastric acid resistance protein and proteins of unknown function (possibly involved in biofilm formation), which might be mechanisms for long-term colonization in the human intestinal tract.

Indexed as

beta-LactamasesEscherichia coliEscherichia coli ProteinsMass SpectrometryMutation, MissenseProteomicsAmino Acid Substitutionbeta-LactamasesEscherichia coli Proteins

Identifiers

PMID31189981
PMCPMC6561927
OpenAlexW2950888461

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

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.