Evidence map›Paper›PMID 39666758›Full record

ArticlePLoS pathogens2024

Deep phosphoproteomics of Klebsiella pneumoniae reveals HipA-mediated tolerance to ciprofloxacin.

Payal Nashier, Isabell Samp, Marvin Adler, Fiona Ebner, Lisa Thai Lê, Marc Göppel, Carsten Jers, Ivan Mijakovic, Sandra Schwarz, Boris Macek

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PLoS pathogens, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Exploration of Phosphoproteins inPathogens (Basel, Switzerland) · 2025
    Article
  2. 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

10 authors.

Payal NashierProteome Center Tübingen, Institute of Cell Biology, University of Tübingen, Tübingen, Germany.
Isabell SampInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Institute of Medical Microbiology and Hygiene, University of Tübingen, Tübingen, Germany.
Marvin AdlerInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Institute of Medical Microbiology and Hygiene, University of Tübingen, Tübingen, Germany.
Fiona EbnerInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Institute of Medical Microbiology and Hygiene, University of Tübingen, Tübingen, Germany.
Lisa Thai LêInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Institute of Medical Microbiology and Hygiene, University of Tübingen, Tübingen, Germany.
Marc GöppelInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Institute of Medical Microbiology and Hygiene, University of Tübingen, Tübingen, Germany.
Carsten JersThe Novo Nordisk Foundation, Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, Denmark.
Ivan MijakovicThe Novo Nordisk Foundation, Center for Biosustainability, Technical University of Denmark, Kongens Lyngby, Denmark.
Sandra SchwarzInterfaculty Institute of Microbiology and Infection Medicine Tübingen, Institute of Medical Microbiology and Hygiene, University of Tübingen, Tübingen, Germany.
Boris MacekProteome Center Tübingen, Institute of Cell Biology, University of Tübingen, Tübingen, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Klebsiella pneumoniae belongs to the group of bacterial pathogens causing the majority of antibiotic-resistant nosocomial infections worldwide; however, the molecular mechanisms underlying post-translational regulation of its physiology are poorly understood. Here we perform a comprehensive analysis of Klebsiella phosphoproteome, focusing on HipA, a Ser/Thr kinase involved in antibiotic tolerance in Escherichia coli. We show that overproduced K. pneumoniae HipA (HipAkp) is toxic to both E. coli and K. pneumoniae and its toxicity can be rescued by overproduction of the antitoxin HipBkp. Importantly, HipAkp overproduction leads to increased tolerance against ciprofloxacin, a commonly used antibiotic in the treatment of K. pneumoniae infections. Proteome and phosphoproteome analyses in the absence and presence of ciprofloxacin confirm that HipAkp has Ser/Thr kinase activity, auto-phosphorylates at S150, and shares multiple substrates with HipAec, thereby providing a valuable resource to clarify the molecular basis of tolerance and the role of Ser/Thr phosphorylation in this human pathogen.

Indexed as

Anti-Bacterial AgentsBacterial ProteinsCiprofloxacinKlebsiella pneumoniaeProteomicsDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsHumansKlebsiella InfectionsPhosphorylationProtein Serine-Threonine KinasesProteomeAnti-Bacterial AgentsBacterial ProteinsCiprofloxacinEscherichia coli ProteinsProtein Serine-Threonine KinasesProteome

Identifiers

PMID39666758
PMCPMC11717353

What OpenQuestion holds

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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.